th  - 1988 - 51st ENC Conference

29 th �� - 1988 Rochester 

Chair: Stanley Opella 

Local Arrangements: Nick Zumbulyadis 

There was some concern about the northern location selected for 

the 29th ENC. Fortunately, Rochester New York lived up to its 

reputation as the Flower City by having unseasonably warm 

weather in April of 1988. Notably, this was the first ENC 

organized by Judith Sjoberg and her Science Managers company, 

and this relationship has had a profound effect on all subsequent 

ENCs by ensuring that the meeting arrangements are of the same 

high quality as the scientific presentations. Also, this meeting led 

to the ENC being included on the New York Times list of key 

meetings on the scientific speaker's circuit. 

Twenty years have passed since the 29th ENC, and this is the first 

time that I have looked at the scientific program since the meeting 

was held. I am struck by the prescience of so many of the presentations. There were entire sessions 

devoted to magic angle sample spinning, ordered biological systems, and dynamic nuclear 

polarization, in addition to those in the more general areas of pulse sequence development, 

materials and biological imaging, and things that now would be referred to as exotica. 

The magic angle sample spinning session introduced a number of advances that have transformed 

this field of research. It started with a talk on NMR strategies and high-speed MAS by Gary Maciel, 

which could be given today until you notice that the abstract mentions speeds “inching toward 30 

kHz.” The experimental NMR methods discussed in the talks Measurements of two-dimensional 

NMR powder patterns in rotating solids (Takehiko Terao), 13 C- 15 N Rotational Echo Double 

Resonance (Jake Schaefer), and Rotational Resonance in solid state NMR (Bob Griffin) are still 

being refined and combined to provide the pulse sequences applied in contemporary studies of 

polycrystalline proteins. 

In the session on ordered biological systems, two of the talks were particularly notable for where 

they have led. In the talk Multinuclear experiments for the determination of oligosaccharide 

structure in liquid crystal phases, Jim Prestegard described how orientational information could be 

obtained from weakly aligned biomolecules through measurements of what would become residual 

dipolar couplings, now an essential element of nearly all protein NMR studies in solution. And Tim 

Cross used his talk Dynamics of Gramicidin A transmembrane channel by solid state 15 N NMR to 

introduce the interplay of structure and dynamics that dominate current solid-state NMR studies of 

aligned membrane proteins. 

The Program for the 29th ENC reflected the input of the NMR community and discussions and 

compromises among the members of the Executive Committee. At the time of the meeting, I 

thought it went well, and the participants I heard from were complimentary. I didn't reflect on the 

quality of the meeting during the intervening twenty years. Now, my reaction is one of 

astonishment. The scientific presentations were so far ahead of their time, that it took a while for 

them to have their impact. The credit for the success of the 29th ENC belongs solely with the 

practitioners of experimental NMR spectroscopy who showcased their ideas and results in 

Rochester.

. r 

ENC, I . 

29th Experimental Nuclear Magnetic Resonance Spectroscopy Conference 

Rochester, New York, April 17-21, 1988 

Conference Office 

750 Audubon 

East Lansing, MI 48823 

(517) 332-3667 

Executive Committee 

Stanley J. Opella, Chair 

University of Pennsylvania 

Department of Chemistry 

Philadelphia, PA 19104 

(215) 898-6459 

A.N, Garroway, Chair-Elect 

Naval Research Laboratory 

Code 6120 

Washington, DC 30375 

(202) 757-2323 

N. Zumbulyadis, Local Arrangements 

Eastman Kodak Company 

Corporate Research Laboratories 

Rochester, NY 14650 

(716) 722-1409 

Edward O. Stejskal, Secretary 

North Carolina State University 


Raleigh, NC 27695 

(919) 737-2998 

Mary W. Baum, Treasurer 

Princeton University 


Princeton, NJ 08544 

(609) 452-3892 

Lynne Batchelder 

Ad Bax 

Bernhard Bluemich 

Jo-Anne K. Bonesteel 

R. Andrew Byrd 

Paul W. Cope 

Colin Fyfe 

Myra Gordon 

Lynn Jelinski 

Gary E. Maciel 

Charles G. Wade 

Welcome to the 29th ENC! 

It is a pleasure to welcome all participants to Rochester for the 29th 

ENC. Just as the month of April invariably presages the May bloom in 

Rochester, the Flower City, the fecund discussions at the ENC always lead 

to new research in experimental NMR spectroscopy. 

The high quality and originality of the abstracts for the oral and poster 

presentations demonstrate that the ENC continues as the premier forum for 

the field of experimental NMR spectroscopy. These abstracts provide an 

instant snapshot of this vigorous and dynamic field. The program is 

described in this notebook with the abstracts for the oral presentations near 

the schedule and the poster abstracts in a separate section. All of the talks will 

be given in the North Exhibition Hall. All posters should be set-up on 

Sunday in the Lilac Ballroom of the Convention Center and remain up 

throughout the meeting; they should be taken down after the 5:30 pm closing 

of the Wednesday afternoon poster session. The presenters of posters with 

even numbered abstracts should be at their posters between 2:30 pm and 

5:30 pm on Monday and the presenters with odd numbered abstracts between 

2:30 pm and 5:30 pm on Wednesday. 

The ENC also provides many opportunities to renew old friendships and 

to establish new ones. Please be sure to wear your registration badge during 

all scientific and social activities. There will be a Welcome Reception 

Sunday evening beginning at 7:00 pm in the Convention Center Galleria. 

There are coffee breaks between morning sessions. Lunch will be served in 

the South Exhibition Hall. Consult the enclosed restaurant guide for insight 

into the local gourmet scene. All hospitality suites are located in the 

Convention Center and Holiday Inn. They will close at 2:00 am in accord 

with local ordinances. The Conference Cocktail Party will be held between 

6:00 pm and 7:00 pm on Wednesday in the Ballroom Foyer on the second 

level of the Rochester Plaza Hotel and is open to all participants. 

All comments and suggestions are welcome and will help A1 Garroway, 

Chair of the 30th ENC, plan the meeting for April 2-6, 1989 at the Asilomar 

Conference Center in Pacific Grove, California. 

Please join me in participating in a successful 29th ENC, 

Chair, 29th ENC

PROGRAM: This conference program has divided 

lectures and posters into two sections. The abstracts 

of presentations appear in the appropriate section. The 

author index is located in an additional section. The 

index references the page number where the abstract 

appears. 

Presentors of oral papers should arrive about 15 

minutes before the session is scheduled to begin. If you 

are using slides, please give them to the projectionist 

before the start of the session. 

Posters have been numbered. If your poster is an even 

number, you must be present in the poster session on 

Monday afternoon. If your poster is an odd number, you 

should be present at the Wednesday session. 

Posters should be mounted on Sunday evening. All 

poster spaces have been numbered. Please be sure 

to mount your poster in the space that corresponds to 

your poster number in the program. 

LOCATION OF SESSIONS: Oral sessions are in the 

North Exhibit Hall. Poster sessions are in the Lilac 

Ballroom. 

EMPLOYMENT CENTER: The employment center will 

maintain a file of resumes. If you wish to register, please 

come to the center on Monday morning. Notices of 

employment positions may be placed on the bulletin 

board designated for that purpose. 

REGULATIONS: The following regulations are in the 

best interests of the conference: 

. No smoking in any session, including the poster 

sessions. 

. Registration badges must be worn to all con- 

ference activities, including hospitality suites, the 

welcome reception, and the Wednesday cocktail 

party. 

The 29th ENC 

Rochester, New York 

April 17-21, 1988 

. Your cooperation is requested in closing hospitali- 

ty suites at 2:00 a.m. in compliance with 

Rochester liquor laws. 

. The opening of hospitality suites should not 

conflict with conference sessions. 

HOSPITALITY SUITES: Hospitality suites are located 

in the Holiday Inn, as well as the Convention Center. 

The suites in the Holiday Inn are on the mezzanine level 

(same level as the skywalk) and in parlors on the upper 

floors. 

CONFERENCE REFRESHMENTS: Coffee Breaks will 

be available on Monday, Tuesday, Wednesday and 

Thursday mornings in the GaUeria of the Convention 

Center at the times indicated in the program. 

There will also be refreshments served during the poster 

sessions on Monday and Wednesday afternoons. 

LUNCH: A cafeteria-style lunch may be purchased in 

the South Exhibit Hall. With the number of people 

expected to use this service, long lines at the beginning 

are inevitable. However, the crowd will be served as 

efficiently as possible. Please be patient. 

If you prefer to go out for lunch, a restaurant guide is 

located in this program. 

NIAGARA FALLS EXCURSION: The Niagara Falls 

excursion buses will load at the (~onvention center main 

entrance between 12:15 and 12:30 p.m. Lunch will be 

served on board the buses. Non-U.S. citizens must bring 

a passport or appropriate papers for Canadian customs. 

The buses will return at approximately 6:30 p.m. 

COCKTAIL PARTY: The cocktail party hosted by 

Varian Associates will be in the Rochester Plaza Hotel 

(across the river). It will be in the ballroom foyer, second 

level, between 6 and 7:00 p.m. 

2

The Executive Committee of the 29th ENC 

gratefully acknowledges the financial support for 

the conference from the following organizations: 

Academic Press 

Aldrich Chemical 

Amplifier Research 

Bruker 

Cambridge Isotope Laboratories 

Chemagnetics 

Chemical Dynamics 

Creative Electronics 

Dory Scientific 

Drusch 

Eastern Analytical Symposium 

Electronic Navigation Industries 

GE NMR instruments 

IBM - Almaden Research Center 

ICN 

ICON Services 

Isotec 

JEOL 

Eastman Kodak 

Merck Sharp and Dohme Isotopes 

M-R Resources 

Nalorac Cryogenics 

New Era Enterprises 

New Methods Research 

Norell 

Oxford Instruments 

Pergamon Journals 

Phospho-Energetics 

Sciteq 

STN International 

Siemens Medical Systems 

Spectral Data Services 

Spectroscopy Imaging Systems 

Stevens Creek Software 

Tecmag 

Varlan Associates 

Wilmad Glass 

John Wiley & Sons 

Xerox

The Executive Committee of the 29th ENC 

gratefully acknowledges financial support for 

underwriting the following: 

Isotec 

Program binders 

Programmed Test Sources 

Tote bags 

Amplifier Research and Programmed Test Sources 

Welcome reception 

Stanley J. Opella, Chair 




(215) 898-6459 

A.N. Garroway, Chair-Elect 


Code 6120 


(202) 747-2323 

N. Zumbulyadis, Local Arrangements 


Corporate Research Laboratories 


(716) 722-1409 

Edward O. Stejskal, Secretary 

North Carolina State University 


Raleigh, NC 27695 

(919) 737-2998 

Bruker Instruments 

Coffee breaks 

GE NMR Instruments 

Monday Poster refreshments 

JEOL 

Wednesday Poster refreshments 

Varian Associates 

Wednesday cocktail party 

EXECUTIVE COMMITTEE 

4 

Mary Wo Baum, Treasurer 




(609) 452-3892 

Lynne Batchelder 

Ad Bax 


Jo-Anne K. Bonesteel 


Paul W. Cope 

Colin Fyfe 

Myra Gordon 

Lynn Jelinski 

Gary E. Maciel 

Charles G. Wade

101 

101 

101 

101 

101 

101 

101 

VENDOR SUITE LOCATIONS 

101 J 

101 K 

102 A 

102 

102 

102 

103 

103 

103 

103 

A 

B 

C 

D 

E 

F 

G 

C 

D 

E &F 

A 

B 

C 

D 

&H 

&B 

Exchange 

Fairfax 

Genessee 

Huron 

Tiffany 

1425 

1500 

1200 

925 

CONVENTION CENTER 


Chemagnetics 


Doty Scientific 


Electronic Navigation Industries 


M-R Resources 


JEOL, USAJLtd 

Intermagnetics General 

Tecmag 


ICN Stable Isotopes 

Chemical Dynamics 

Sciteq 

Phospho-Energetics 

HOLIDAY INN MEZZANINE 

ICON Services 

Cambridge Isotope Laboratories 

Programmed Test Sources 

Amplifier Research 

Merck Sharp & Dohme 

Isotec 

HOLIDAY INN SUITES 

Nalorac 

Oxford Instruments 

Wilmad Glass 

STN International

A 

A 

0 

0 

,-..1 

I 

Z 

Z 

0 

"c 

N 

"1" 

i 

0 

,.I 

Q. 

Q. 

....... :" " " J U J '.a~ 

Ji~ E!-~ ..... 

~--J: - El-i . 

J ~ F1 

t 

. . . . 

....... .1~- ]:-' ~ °' 

, 

L~ 

>-, 

rd~ 

X 

I~o .,.-i 

c~ r.z., 

u 

X 

LT4

i 

L 

3~,.ols I 0', 

I 

===~ ~ F',~ R ', : tl - I! 

U ' II 

I 4 U I 

n , H ~, ~/.., < ++ R+, 

",l u", n LlOS ~-olbm~ ~i~-niP', 

°~ L 

0 

0 

Z 

rr u 

c/] 

0 

0 

~9 

0 

E 

I- ,,,=I l.,,m- , 

°mlll 

= Ii 

=0 0 0 

30vN3nOl~ 

o o 

Z 

u~ 

0,-~ 

I---I 

~0 

0 

u 

0 

0 

0 0 

---r ~-+-T '+++ " 

£33~£$ tlv~ 

Z 

]oo 

u-I 

0~0 u~ 

u-I ~x4 

o i c'm.,~F 

w 

0 

r._) 

----I 

I

Restaurants in Rochester 

Restaurants close to the Convention Center are located in some unlikely 

places. This selection is intended to help you find them. No claims are made as 

to completeness, and you may very well find a restaurant you like that is not on 

the list. Within about a mile of the Convention Center there are many more 

eating places than there are in the immediate downtown area. With a car or 

some extra time you may want to try some of the outlying places mentioned at the 

end of the list. 

First for the more exoensive olaces. In Rochester this means about $25 for 

a full meal. exceot where noted. 

The first revolving restaurant in New York, The Changing Scene, is 

located on the top floor of First Federal Plaza, the tall building next to the 

Rochester Plaza. 

Chapel's is located in the former City Hall, a renovated historic setting. 

is very good, but in the evening you will spend at least $40 per person, and the 

meal usually spans several hours. 

Edwards at 13 S. Fitzhugh is just off Main street, several blocks west of 

the river. It is one of the well-established, quality restaurants in Rochester, but is 

also likely to be more expensive than most. 

Joseph's is a good Italian restaurant located at 169 N. Chestnut, about a 

block from the Eastman Theater. The prices are well within reason. 

The Riverview Cafe in the Rochester Plaza is also a good choice. 

Meals in the moderate ranae should run about $15. 

An excellent oriental restaurant is the Bangkok, 155 State Street, across 

from the Rochester Plaza. It has both a Chinese and a Thai menu, and will give 

you a 5% discount on evening meals if you show your registration card. Lunch is 

at the menu price. 

Beams Restaurant, 106 Andrews Street at the corner of St. Paul one 

block north of the Holiday Inn is pleasant. Some of their menu items have a 

"health-food" note. 

A new restaurant that comes with good recommendations is The Filling 

Station. The building formerly was just what it says. It is located at 30 Mount 

Hope Ave., just across the Inner Loop. 

Trebor's, on State Street across from the Rochester Plaza, is popular 

among the business crowd at lunch. 

It

Gellert's, next door to the Eastman Theater on Gibb's Street has a 

simple, but pleasant atmosphere. It caters in large part to the theater crowd. 

Sibley's, one of the downtown department stores, has a surprisingly 

good restaurant on its top floor, as well as snack bars and a pastry shop on the 

ground floor. In McCurdy's are the Garden Room and Oak Room. 

If you have a reallv tiaht budoet, there are also some choices. 

There are a couple of soup and sandwich places in Midtown Plaza, 

which used to be several downtown city blocks and now is a completely 

enclosed shopping mall located at Main and Clinton, two blocks east of the 

Convention Center. Try the Great Canadian Soup Company. There is also 

a Burger King in this complex. The Top of the Plaza (take the elevator) 

does not fall in the inexpensive class, but is reputed to have good hamburgers for 

lunch and would be good for a more expensive evening meal.. 

There are McDonalds on Main Street, about one block east of the 

Convention Center, and on State Street, across the street from the Rochester 

Plaza. 

Sweet Dawn's, at the corner of Main Street and Stone, is good for soup 

and sandwiches. 

Across State Street from the Kodak Office building is Rubino's, selling 

submarine sandwiches and the associated items. Rubino's also runs the 

Salumeria Care in Midtown Plaza. 

If you want to aet a little further from the Convention Center, look on 

Alexander Street, whi-ch crosses East Avenue on the other Side of the Inner Loop, 

on Park Avenue, which crosses Alexander about a block south of East Avenue, 

or on Monroe Avenue, which crosses Alexander still further South.. Some of the 

restaurants on Alexander are rather expensive. The Park Avenue area is a bit 

"yuppie" and spills over onto Monroe. The best restaurant bargains are probably 

on Monroe. Several different ethnic groups are represented. 

If YOU have a car. there is a wide choice of restaurants. You might want to 

try the Spring House, 3001 Monroe Avenue (take the freeway), an inn that 

originally was located next to the Erie Canal. (The canal moved; the restaurant is 

where it always was, but if you look closely off to the side behind the building you 

can see a trace of the old ditch.) On the present-day canal, but much further out, 

is Richardson's Canal House, 1474 March Road, the only restaurant in 

Rochester listed in the Mobil guide. 

9

8:30 a.m. 

8:35- 10:05 

10:05 - 10:25 

10:25- 12:15 

12:15 p.m. 

2:30 - 5:30 

7:30 - 9:30 

8:30 - 10:20 a.m. 

10:20 - 10:40 

10:40- 12:10 

12:10 p.m. 

12:15- 12:30 

7:30 - 9:30 

MONDAY, APRIL 18, 1988 

PROGRAM 

Opening remarks, S. J. Opella, Chair. 

Low Temperatures end Fields. 

G. Maciel, Session Chair. 

North Exhibit Hall. 

Coffee Break. 

Convention Center Gaileria. 

Compliments of Bruker Instruments. 

Magic Angle Sample Spinning. 

E. Stejskal, Session Chair. 


Lunch. A cafeteria style lunch may be purchased in the South Exhibit Hall. 

Poster Session. 

Lilac Ballroom. 

Authors of even numbered posters present. 

Refreshments compliments of GE NMR Instruments. 

Detection and Analysis. 

M. Baum, Session Chair. 


TUESDAY, APRIL 19, 1988 

PROGRAM 

Two-Dimensional Spectroscopy. 

C. Wade, Session Chair. 


Coffee Break. 

Convention Center Galleria. 

Selective Pulse Sequences. 

A. Bax, Session Chair. 

Lunch. A cafeteria-style lunch may be purchased in the South Exhibit Hall. 

Niagara Falls Excursion buses depart. 

Lunch will be served on the buses. 

Afternoon free! Don't miss the George Eastman House Containing the International 

Museum of Photography, or walk along the river to view the Falls. 

High Tc Superconductors. 

L. Jelinski, Session Chair. 


11

8:30 - 10:10 a.m. 

10:10- 10:30 

10:30- 12:10 

12:10 p.m. 

2:30 - 5:30 

6:00 - 7:00 

7:00 p.m. 

8:30 - 10:05 a.m. 

10:05- 10:25 

10:25 o 12:05 

WEDNESDAY, APRIL 20, 1988 

PROGRAM 

Materials Imaging. 

A. Garroway, Session Chair. 


Coffee Break. 


Biological Imaging. 

R. A. Byrd, Session Chair. 


Lunch. A cafeteria-style lunch may be purchased in the South Exhibit Hall. 

Poster Session. 

Authors of odd numbered posters present. 

Refreshments compliments of JEOL. 

Cocktail party. 

Rochester Plaza Hotel, Ballroom Foyer. 

Compliments of Varian Associates. 

Open to all conference registrants. 

Conference Banquet. 

The Future of Conventional and Electronic Imaging; 

Robert Hunt, University of London. 

Rochester Plaza Ballroom. 

Tickets required. 

THURSDAY, APRIL 21, 1988 

PROGRAM 

Ordered Biological Systems. 

L. Batchelder, Session Chair. 


Coffee Break. 


Dynamic Nuclear Polarization. 

N. Zumbulyadis, Session Chair. 


Conference Adjourned. 

See you next year at Asilomar, April 2-6, 1989. 

12

8:30 a.m. 

8:35 a.m. 

9:05 a.m. 

9:15 a.m. 

9:25 a.m. 

9:35 a.m. 

10:05 a.m. 

MONDAY MORNING 

LOW TEMPERATURES AND FIELDS 

G. Maciel, Session Chair 

Opening remarks, S. J. Opella, Chair. 

T 1 Mechanisms of Solids Immersed in 3He. 

O. Gonen, P. L. Kuhns, *J. S. Waugh. 

Untruncation of Dipole-Dipole Couplings in Solids, 

or Zero Field NMR Entirely in High Field. 

R. Tycko. 

Interpretation of the NMR Nutation Spectra. 

*A. Samoson, E. Lippmaa. 

High Resolution Electrophoretic NMR (ENMR) of a Mixture. 

*T. R. Saarinen, C. S. Johnson. 

Collaborative Projects in NMR. 

A. Pines. 

Break. 

13

cON 8:35 ] 

It. 

T 1 MECHANISMS OF SOLIDS IMMERSED IN 3He 

O. Gonen, P.L. Kuhns, and J.S. Waugh*, MIT, Cambridge, MA. 02139 

Spins (I) at the surface of a solid can be relaxed by neighboring 3He 

spins. Thereafter the interior of the solid is relaxed through spin diffusion. 

ForQ|gn (S) spins in the surface layer inhibit the escape of I-magnetization 

to the interior, and S spins distributed throughout the bulk may inhibit spin 

diffusion altogether. A variety of 1H, 2H, and 29Si measurements in Si02 

i11ustrate and quantify these effects. Examples will be presented of selective 

spectroscopy of adsorbed species in sub-monolayer coverage. 

14

f~ 

I UNTRUNCATIO~I OF DIPOLE-DIPOLE COUPLINGS IN SOLIDS, OR ZERO FIELD 

MON 9:0S I NMR ENTIRELY IN HIGH FIELD. Robert Tycko, AT&T Bell Laboratories, 

Murray Hill, Nj, 07974. 

N::R spectra of powdered or noncrystalline solids in high field commonly exhibit broad 

lines that arise from the dependence of the nuclear magnetic dipole-dipole couplings 

on molecular orientation. New experiments will be described in which that orientation 

dependence is removed by the combination of rapid sample rotation with a synchronized 

rf pulse sequence.• The sample rotation and pulse sequence have the effect of con- 

verting the usual truncated dipole-dipole couplings into an untruncated form. The 

result is N,~IR spectra with sharp lines and splittings that depend only on inter- 

nuclear distances, i.e. spectra with a "zero field" appearance that are obtained 

entirely in high field. Such spectra provide a means of studying molecular conforma- 

tions in solids, without requiring single crystals. The theory behind untruncation 

experiments will be presented along with experimental spectra of simple organic 

solids. 

15

[--~N 9:15 

INTERPRETATION OF THE NMR NUTATION SPECTRA. A. Samoson * and E. 

I Lippmaa, Institute of Chemical Physics and Biophysics, Estonian 

Academy of Sciences, 200001Tallinn, USSR. 

The quadrupole interaction parameters of half integer spin nuclei are 

accessible from the dependence of NMR central transition signal on the rf excitation 

pulse length. The Fourier analysis yields (nutatlon) spectra, consisting at most 

of 21 major lines. The lines can be associated with single quantum coherences in a 

rotating magnetic field created by the rf pulse. The magnetization vectors 

describing spin evolution in the rotating magnetic field nutate in different senses, 

depending on the quantum numbers of respective energy levels. This provides for 

further unravelling of 2D spectra via hypercomplex Fourier transform. The ratio of 

a first moment to integral intensity of the nutation spectra gives a good estimate 

for the quadrupole interaction constant. The nutation spectroscopy applied to the 

study of zeolites, glasses and organic conductors provided for identification of 

various nuclear sites and interpretation of complicated ID spectra. 

Current address: Department of Chemistry, University of California, Berkeley, 

CA 94720. 

16

MON 9:25 

HIGH RESOLUTION ELECTROPHORETIC ~ (ENMR) OF A MIXTURE: 

Timothy R. Saarlnen' and~les S. Johnson, Jr., University of North 

Carolina, Dept. of Chem., Chapel Hill, NC 27599-3290 

Electrophoretic mobilities have been measured in situ using 

pulsed field gradient NMR (PFGNMR). Several components in a mixture 

can be studied simultaneously by Fourier transformation of the second 

half of the spin echo. For a U-tube configuration application of an 

electric field across the sample resu/ts ~n a cosinusoidal modulation 

of spectral peak amplitudes, cos(Kv= t) where K equals the area of the 

gradient pulse times the gyrcmagnetic ratio, v: is the drift velocity 

of the i'th species, and t is the duration of the electric field 

pttlse. By working at low ionic strengths electric fields of up to 50 

V/cm could be applied for i sec before convection ~as detected by a 

change in the amplitude of the HOD peak. The cationic mobilities in 

a mixture of tetra-methyl and tetra-ethyl anmonJum chloride in D20 

were determined. Application of the technique for studying emulsions 

looks prc~lising. 

17

IION 9 : 35 [ 

COLLABORATIVE PROJECTS IN NMR: A. Pines, University of Califomia, 

Berkeley, CA 94720 

Topics for discussion will be selected from among the following: 

1. Quantum phase of the photon and its relevance to magnetic resonance. 

2. Multiple-pulse NMR in zero field. 

3. Zero field NMR studies of small local asymmetries. 

4. 2-Dimensional studies of molecular conformations in liquid crystals. 

5. Clustering of molecules in zeolites studied by Xenon and multiple-quantum NMR. 

6. Detection of quadrupole resonance by a SQUID detector at low temperature. 

7. Iterative spin decoupling schemes for solids. 

8. High-temperature NMR of silicate glasses and liquids. 

Some of these projects are carried out in collaboration with M.V. Berry 

(Physics, Bristol); J. Clarke (Physics, Berkeley); J. Fraissard (Chemistry, Paris); J. 

Guckenheimer (Mathematics, Cornell); C.J. Radke (Chemical Engineering, Berkeley) 

and J. Stebbins (Geology, Stanford). 

18

• . r, 

10:25 a.m. 

10:55 a.m. 

11:05 a.m. 

11:35 a.m. 

11:45 a.m. 

12:15 p.m. 

MONDAY MORNING 

MAGIC ANGLE SAMPLE SPINNING 

E. Stejskal, Session Chair 

NMR Strategies and High-Speed MAS. 

*G. E. Maciel, C. E. Bronnimann, 

S. F. Dec, B. L. Hawkins, R. A. Wind. 

Measurements of Two-Dimensional NMR Powder Patterns in 

Rotating Solids. 

T. Nakai, J. Ashida, *T. Terao. 

13C-lSN Rotational Echo Double Resonance. 

T. Gullion, *J. Schaefer. 

2D Chemical Shift Anisotropy Correlation Spectroscopy. 

A new Sample Positioning Mechanism Which Simplifies 

Measurement of Chemical Shift Anisotropies in Complex 

Single Crystals. 

M. H. Sherwood, *D. W. Alderman, 

D. M. Grant. 

Rotational Resonance in Solid State NMR. 

D. P. Raleigh, M. H. Levitt, 

F. Creuzet, *R. G. Griffin. 

Lunch. 

19

MON i0:25 

NMR STRATEGI'ES AND HIGH-SPEED MAS, G.E. Maciel * C.E. Bronnimann 

, 9 

S.F.Dec, B.L. Hawkins and R.A. Wind, Department of Chemistry, 

Colorado State Univesity, Ft. Collins, CO 80523 

With MAS speeds inching toward 30 KHz, a variety of important possibilities 

and issues arise in solid-state NMR. One of the most direct benefits of high-speed 

MAS is the ability to reduce spinning sidebands and r~e~move them from spectral 

regions of interest. This is especially beneficial in ~'Al NMR, allowing the use 

of high fields with the corresponding reduction in the second-order quadrupole 

effect. Examples will be shown. 

The temptation to employ high-speed MAS as a high-resolution ~oli~-state IH 

NMR technique must be considered in relation to the nature of the~H-~H dipolar 

interactions in each sla~_P1~e ~ Direct comparisons of CRAMPS and MAS only r,~ults 

show that when strong ipolar interactions are present, as expected, the 

CRAMPS approach provides far superior results. 

The anticipated interference of high-speed MAS with CP efficiency i ~H r ~ dily 

demonstrated, even in systems with strong dipolar interactions. In - C CP 

experiments carried out as a function of MAS speed, the Hartmann-Hahn match curves 

differ dramatically for carbons with directly attached hydrogens relative to carbons 

without. Hence, the use of high-speed MAS to overcome spinning sideband 

problems in high-field CP-MAS experiments seems problematical. One potential 

approach to this kind Of problem may be stop-and-go (STAG) spinning, in which CP 

occurs during a static-sample period in the STAG-sequence. Some STAG results will 

be shown. 

20

~'-O-i 0 N i0:55 

MEASUREMENTS OF TWO-DIMENSIONAL NMR POWDER PATTERNS IN ROTATING 

ISOLIDS.T. Nakal, J. Ashida and T. Terao , Department of Chemistry, 

Faculty of Science, Kyoto University, Kyoto 606, Japan. 

Switching-angle sample-splnnlng techniques for measuring the heteronuclear 

dipolar/chemlcal shift 2D powder patterns are reported. The techniques have the 

advantages of the high slgnal-to-nolse ratio and the low distortion of the spectrum 

compared with those in stationary powder samples. Furthermore, for compounds with 

more than one chemically distinct nucleus, the individual 2D powder patterns can be 

separately obtained by 3D NMR. Practical applications of these techniques are 

demonstrated with the 13C 2D powder patterns of calcium formate, polyethylene, and 

polyacetylene. The chemical shift tensors and proton positions in calcium formate 

were obtained for the two crystallographlcally inequivalent formate ions, which 

agree with the results already reported by single crystal studles of 13C NMR and 

neutron diffraction. The chemical shift principal axes in polyethylene were found 

to be only approximately along the symmetry directions of the CH 2 group, indicating 

a strong perturbation of the electric environment by the crystal field. 


"CA 94720. 

21

I 13C-15N ROTATIONAL ECHO DOUBLE RESONANCE 

~0N 11:05 i 

Terry Gullion and Jacob Schaefer* 

Dept. of Chemistry, Washington Univ., St. Louis, MO 63130 

Dephasing of 13C rotational echos in solids containing pairs of 

dipolar coupled 13C and 15N spins occurs when the sign of the C-N 

interaction is reversed by some trains of 15N ~ pulses with 

periods less than that of the rotor. Fourier transforms of the 

echos with and without the ~ pulses lead to a 13C NMR difference 

spectrum which arises only from those 13C's with 15N neighbors. 

This rotational-echo double-resonance (REDOR) experiment combines 

elements of the spin-echo double-resonance (SEDOR) technique used 

by Slichter to observe 13C-170 couplings in static solids, with 

the dephasing properties of ~ pulse trains used by Lippmaa and by 

Waugh to characterize 13C chemical 

shift tensors in rotating solids. 

REDOR is easier to perform 

than 13C-15N double-cross 

REDOR 

polarization because the 

technically difficult 

H H CP 

DECOUPLE 

Hartmann-Hahn match between weakly ~ 

coupled carbons and nitrogens is c J ~ i 

avoided. In addition, REDOR 

differences can be as much as an N --~ll 

order of magnitude greater than the 

corresponding double-cross rotor i i 

differences for the same 

13C-15N containing sample. 

22 

II II 

N 

W 

I I I 

! ACOUmE 

i 

|

MON 11:3S 12D CHEMICAL SHIFT ANISOTROPY CORRELATION SPECTROSCOPY. A NEW 

SAMPLE POSITIORING MECHANISM WHICH SIMPLIFIES MEASUREMENT OF CHEMICAL SHIFT 

ANISOTROPIES IN COMPLEX SINGLE CRYSTALS. Mark H. Sherwood , D.W. Alderman~ & 

D.M. Grant, Dept. of Chemistry, University of Utah, Salt Lake City, UT 84112 

2D chemical shift anisotropy (CSA) correlation spectroscopy permits the 

measurement of CSA tensors in complex single crystals with far more peaks than 

have been tractable with 1D techniques (1). Such measurements open the 

possibility of using CSA tensors as structural and conformational probes in 

large molecules. The basis of the technique is to obtain 2D spectra in which 

the peaks are located by the chemical shift at two different single crystal 

orientations. The spectra are obtained by moving the crystal between the two 

orientations during the mixing time of a chemical exchange 2D pulse sequence. 

It will be shown how the complete CSA tensors for all the nuclei in a 

complex single crystal can be determined by measuring peak frequencies at only 

six well chosen orientations of the crystal and correlating these measurements 

with the 2D technique. The special geometry of a mechanism to accomplish the 

necessary orientation and reorientation will be explained and the device itself 

installed in a 200 MHz probe exhibited. In order to measure all the tensors in 

a single crystal the sample need be mounted only once in the mechanism and six 

2D spectra obtained. 

Six 2D spectra which determine the carbon-13 CSA tensors in a single 

crystal of sucrose will be shown. Sucrose has 12 carbons per molecule and two 

molecules per unit cell so that 24 peaks are observed. 

The possibilities of the technique for measurement of tensors in 

much more complicated molecules will be discussed. 

(1) C.M. Carter, D.W. Alderman, and D.M. Grant, J. Magn. Reson. 

65, 183 (1985) and 73, 114 (1987). 

23

HON ii :45 

02139 U.S.A. 

ROTATIONAL RESONANCE IN SOLID STATE NMR 

D.P. Raleigh , M.H. Levitt, F. Creuzet and R.G. Griffin 

I Massachusetts Institute of Technology, Cambridge, MA 

In magic angle spinning experiments on samples containing dilute 

homonuclear dipolar coupled spin pairs, rotational resonance (R 2) 

occurs when the spinning speed is adjusted so that the condition 

~iso- = n~ is satisfied. Here ~iso is the difference in isotropic 

r 

chemical shifts, ~ is the spinning speed, and n is an integer. Under 

these conditions t~e fllp-flop term of the dipolar coupling is 

reintroduced into the effective Hamiltonian, and the normally sharp 

resonance lines broaden and split. In addition, a rapid oscillatory 

exchange of Zeeman-order between the dipolar coupled spins is observed. 

The time dependence of the exchange and the spectral lineshapes agree 

with numerical simulations which include the dipolar coupling and the 

relative orientation of shielding tensors. The method is potentially 

useful for estimating through-space dipolar couplings, and therefore 

internuclear distances in polycrystalline solids. 

24

7:30 p.m. 

8:00 p.m. 

8:10 p.m. 

8:40 p.m. 

8:50 p.m. 

MONDAY EVENING 

DETECTION AND ANALYSIS 

M. Baum, Session Chair 

Pressure -- An Essential Experimental Variable in NMR 

Studies of the Dynamic Behavior of Chemical Systems. 

J. Jonas. 

The 13C Relaxation Behavior of Ethane Through Its Critical 

Point. 

R. F. Evilia, S. L. Whittenburg, 

*J. M. Robert. 

Flow NMR and DNP Studies of Dense Fluids. 

*H. C. Dorn, T. E. Glass, L. Allen, 

R. Gitti, C. Tsaio, C. Wild, 

C. S. Yannoni. 

The World and Wonders of 3H NMR Spectroscopy. 

P. G. Williams. 

NMR Approaches to Understanding Natural and Synthetic 

Enzymes. 

J. K. M. Sanders. 

25

MON Eve 7:301 PRESSURE - AN ESSENTIAL EXPERIMENT~ VARIABLE IN NMR STUDIES OF 

THE DYNAMIC BEHAVIOR OF CHEMICAL SYSTEMS: Jiri Jonas , University of Illinois, 

Department of Chemistry, Urbana, Illinois. 61801. 

An overview of several high pressure NMR studies performed in our laboratory 

illustrates the essential role of pressure (density) in the investigation of the 

dynamic behavior of chemical systems. After a brief introduction devoted to the 

novel experimental high pressure NMR techniques, two projects are discussed. 

The two examples deal with the application of multinuclear high resolution N-MR 

spectroscopy at high pressure. First, the results of the study (C.-L. Xie, D. 

Campbell, J. Jonas, J. Chem. Phys., in press, 1988) of the dynamical solvent effects 

on the rotation of coordinated ethylene in ~-CsHsRh(CpHA) p demonstrate the unique 

information about the reaction rates in soluti6n-obtaln~d-from the high pressure NMR 

experiments. Second, the pressure effects on the main phase transition, ln L-a- 

dipalmitoyl phosphatidyl vesicles are investigated by proton decoupled lJc natural 

abundance NMR spectroscopy (C.-L. Xie, P. J. Grandinetti, D. Driscoll, A. Jonas, 

J. Jonas, PNAS, in press). 

The concluding remarks emphasize the wide range of problems that can be studied 

by the high pressure NMR techniques. 

26

HON Eve 8:00 

The 13C Relaxation Behavior of Ethane Through Its Critical Point 

Ronald F. Evilia and Scott L. Whittenburg:" Dept. of Chemistry, 

Univ. of New Orleans, New Orleans, La. 70148 

, Jan M. Robert: Dept. of Chemistry, S.G. Mudd Bldg. #6, Lehigh 

Univ., Bethlehem, Pa. 18015 

The longitudinal relaxation time of 13C in the ethane molecule has been 

measured over a temperature range of -i01 to +50°C, for a sample at the 

critical density. T l appears to vary with temperature, as anticipated; 

however, a discontinuity in the relaxation behavior Is apparent at the 

critical point. From the experimental data, the critical constant may 

be obtained. 

27

[---~N Eve 8:10] 

FLOW NMR AND DNP STUDIES OF DENSE FLUIDSz H. C. Dorn , T. E. 

Glass, L° Allen, R° Gittl, C° Tsaio, C° Wild, Department of Chemistry, 

Virginia Polytechnic Institute and State University, Blacksburg, VA 24061 

and C. S. Yannoni, IBM Almaden Research Center, 650 Harry Road, San Jose, CA 

95120. 

Recent experiments in our laboratory have demonstrated that a flowing liquid 

bolus provides a convenient way to independently optimize the "EPR" and "NMR" 

portions of the dynamic nuclear polarization DNP experiment. Specifically, 

flow -H DNP experiments at I0 GHz were found to require only 0.5-4 watts of 

microwave power in order to achieve saturation (s:l) of a given electron spin 

transition for a number of stable spin labels [e.g., tri-t-butylphenoxides, 

nitroxides, etc.). Flow H DNP results and applications will be presented for 

various flowing fluids (e.g., supercritlcal fluids and liquids). In addition, 

a new technique potentially appl~cable for monitoring surfaces, "s011d-liquld 

Intermolecular transfer [SLIT), H DNP" will also he discussed. 

28

THE WORLD AND WONDERS OF 3H NMR SPECTROSCOPY: Philip G. 

MON illiam ," National Tritium Labeling Facility, Lawrence Berkeley Laboratory 75-123, 

Eve 8 4 0 

Omverslty of California, Berkeley, California 94720. 

The NTLF is a national User Facility, funded by the National Institutes of Health. The Facility combines 

he availability of high levels of carrier free tritium gas, extensive radiochemical purification resources, and an 

n-house NMR instrument dedicated to tritium NMR spectroscopy. The NTLF combines its User service 

"unction with core and collaborative research based on the use of hydrogen isotopes. 

Tritium is an excellent nucleus for NMR observation, but NMR applications in the chemical and biological 

;ciences have been very limited in number. "Onepulse" tritium measurements can quickly and cleanly give the 

:hemical shift and relative abundance of tritons in a sample, and in combination with other physical methods 

:an rapidly assure quality control in labelling experiments. In catalysis hydrogen isotope exchange is readily 

nonitored, with the relative incorporation at each position of a substrate yielding specificity rules for the 

:atalyst as well as mechanistic detail. 

Hydrogenation and halogen replacement reactions are the cornerstone of high level tritium labelling 

~rocedures. Little is known about concomitant side-reactions, but these are extremely important when specific 

abelling is required. Observation of tritium NMR peaks from supposedly "unlabelled" positions obviates 

hese extra mechanisms, and allows the choice of appropriate precursors and reaction conditions for the 

iesirccl tritiation. ' ~ 

As one example, allylic methyl exchange in the hydrogenation of [3-methyl styrene to yield n- 

~ropylbenzene is readily detected, and the full range of isotopomers can be distinguished by J-resolved 

;pectroscopy. Secondly, tritio-dehalogenation of 2-chloro-2'-d.eoxyadenosine with pure "1"2 does not give 

~roduct with the theoretical specific activity, and factors influencing this "dilution" may be followed. 

Important and developing uses of tritium NMR spectroscopy include monitoring of the conversion of 

ntermediates in biological systems, studies of substrate binding, and as an aid in spectral elucidation of proton 

qMR spectra. The use of modern multipulse techniques in concert with simple and elegant older sequences 

ms the potential for giving a great deal of conformational and coupling information, through the interaction of 

~-H and 1-H atoms. NMR work at the Tritium Facility is intent on establishing the benefits and problems 

~ssociated with tritium NMR spectroscopy of many diverse substrates - from simple organics to solids and 

nacromolecules. 

29

Eve 8"50] NMR APPROACHES TO UNDERSTANDING 

NATURAL AND SYNTHETIC ENZYMES 

Jeremy K. M. Sanders* 


University Chemical Laboratory 

Lensfield Road 

Cambridge CB2 1EW 

Recent advances in NMR spectroscopy have given us powerful new tools for 

observing and understanding the details of chemical and biochemical transformations. The 

problem faced by the chemist or biochemist is how to choose the best spectroscopic 

s~ategy for solving a particular problem. We must look at each step in the reaction or 

metabolic process from the point of view of individual nuclei: these are our potential 

reporters. Once we know how the shift or coupling environment for each potential reporter 

is likely to change, we can design NMR experiments that select only the spins of interest, 

even ff the sample is a living organism. These ideas will be illustrated by a wide range of 

examples including the following: 

1. An in vivo deuterium NMR study of formaldehyde dismutases in bacterial 

cultures. 

2. Selective 1H and 13C N]V[R measurements of glutathione biochemistry in 

bacterial and mammalian cells. 

3. One- and two-dimensional IH and 13C studies of iigand binding to 'synthetic 

enzymes' based on porphyrins. 

30

8:30 a.m. 

9:00 a.m. 

9:10 a.m. 

9:20 a.m. 

9:50 a.m. 

10:20 a.m. 

TUESDAY MORNING 

TWO-DIMENSIONAL SPECTROSCOPY 

C. Wade, Session Chair 

Patterns and Relaxations. 

P. Pfandler, U. Eggenberger, D. Limat, 

S. Wimperis, J. -M. Bohlen, 

*G. Bodenhausen. 

Two Dimensional Linear Prediction NMR Spectroscopy. 

*H. Gesmar, J. J. Led. 

Multivariate Techniques for Enhancement of Two 

Dimensional NMR Spectra. 

H. Grahn, *F. Delaglio, 

M. W. Roggenbuck, G. C. Levy. 

2D Rot=ing Frame Spectroscopy: New Approaches and 

Prospects. 

*C. Griesinge~ C. Schonenberge~ 

R. R. Ernst, R. Bruschweile~ 

New Twists to Some Old Experiments. 

*A. Bax, D. Marion, L. Lerner, 

R. Tschudin. 

Break. 

31

.TUE 8"30 

J PATTERNS AND RELAXATION: P. pfvandler, U. Eggenberger, D. Limat, S. 

Wimperis, J.-M. BOhlen and G. Bodenhausen, Institut de Chimie Organique, Universit6 

de Lausanne, Switzerland 

Pattern recognition in 2D NMR spectroscopy is rapidly coming of age, to the 

point where the automated analysis of spectra of weakly coupled spin systems with 

well-resolved multiplets no longer presents a genuine challenge. We are now 

turning our attention to strongly coupled spectra, such as arise from dipolar-coupled 

spin systems in liquid crystalline solutions, to double-quantum spectra which suffer 

from inhomogeneous excitation because of unpredictable coupling strengths, and to 

spectra which suffer from extensive overlap due to aliasing as a result of deliberate 

undersampling. 

Dipole-dipole relaxation not only gives rise to the familiar Overhauser effect 

(migration of Zeeman order ), but, in the presence of cross-correlation of pairs 

of dipolar interactions, may give rise to longitudinal three-spin order . 

Such terms, which may reveal information about angles subtended by internuclear 

vectors, can be observed selectively by means of triple-quantum filtration 

techniques. Cross-correlation can also lead to unexpected coherence transfer 

pathways, particularly when both chemical shift anisotropy and dipolar interactions 

are involved. 

32

TWO DIMENSIONAL LINEAR PREDICTION NMR SPECTROSCOPY 

TUE 9:00 [ , 

Henrik Gesmar and Jens J. Led 

University of Copenhagen, Dept. of Chemical Physics 

The H.C. Orsted Institute, 5, Universitetsparken 

DK-2100 Copenhagen, Denmark. 

Linear prediction has been introduced into the field of NMR spectroscopy as a valu- 

able method of quantitative spectral estimation (1,2). Its applicability has been de- 

monstrated even in case of broad band spectra with many narrowly spaced resonances (3 

l_'.e, cases where LSQ curve fitting procedures (4) would seem to be unfeasible. 

In the present study it is demonstrated that the application of the linear predic- 

tion principle can be extended to include two dimensional NIIR spectroscopy, without 

increasing the computation time drastically. 

Examples are presented and the advantages as well as the pitfalls of the procedure 

are discussed. 

(I) H. Barkhuijsen, R. de Beer, W.M.M.j. Bov6e, and D. van Ormondt, 

J. Magn. R eson. 6_~I, 465 (1985). 

(2) J. Tang, C.P. Lin, I.I.K. Bov~nan, and J.R. Norris, J. Hagn. Reson. 6_22, 167 (1985). 

(3) H. Gesmar and J.J. Led, J. Magn. Reson. (1988). In press. 

(4) F. Abildgaard, H. Gesmar, and J.J. Led, J. Magn. Reson. (1988). In press.

TUE 9:10 

MULTIVARIATE TECHNIQUES FOR ENHANCElVlENT 

OF TWO DIMENSIONAL NMR SPECTRA 

Hans Grahn, Frank Delaglio °, Mark W. Roggenbuck and George C. Levy 

NMR and Data Processing Laboratory, NIH Resource and CASE Center, 

Syracuse University, Syracuse 13244-1200. 

By using multivariate representations of 2D NMR spectra, we show that systematic noise 

such as tl and t2 ridges can be modeled by a Principal Component Analysis (PCA) method. 

Later these noise models can be subtracted from the original data without distorting the 

spectral features. 

In addition, PCA can generate reconstructions of 2D spectra, which are solely based on the 

systematic information from the data, and thus exclude random noise. Special data 

transformations can be applied in conjunction with PCA in order to emphasize or reduce 

specific features; this approach is employed in a diagonal suppression scheme for 2D NOE 

spectra. All of these methods can be combined to optimize data in preparation for 

automated, multivariate-based spectral analysis procedures, which benefit greatly from such 

improvements. 

34

TUE 9"20 ] 

2D ROTATING FRAME SPECTROSCOPY NEW APPROACHES AND PROSPECTS: C. 

Griesinger, C. SchOnenberger, R. Briischweiler, W.O. Scrensen, and R.R. Ernst, 

Laboratorium fiir Physikalische Chemie, EidgenOssische Technische Hochschule, 

8092 Ziidch, Switzerland 

The general potential of rotating frame spectroscopy is explored in view of the 

elucidation of structure and the study of molecular dynamics. Cross relaxation, 

coherence transfer, as well as spectral features in the rotating frame show 

properties distinct from those in the laboratory frame that can be exploited for 

molecular studies. Several techniques have been described so far that involve 

rotting frame concepts. In this lecture, a unified treatment of rotating frame 

experiments is applied and new sequences with improved performance are 

presented. 

It is known that the standard techniques of rotating frame spectroscopy suffer 

from interference of coherent and incoherent transfer processes. New types of 

mixing sequences allow the exclusive selection of a single mechanism. This can lead 

to a more accurate quantification of transfer rates. The new approaches are 

illustrated by application to biomolecules. 

The potential of more exotic rotating frame techniques is discussed. 

Experiments involving transfer of higher spin order in the rotating frame or 

frequency-selective spin locking are conceivable. The incorporation of rotating 

frame and laboratory frame sequences into 3D expcriments will be illustrated by 

protein spectra. 

35

I TUE 9:50 I NEW TWISTS TO SOME OLD EXPERIMENTS 

Ad u=u~, . . uumln~H~e . . . . Marlon, Laura lamer and Rolf Tschudin 

Laboratory of Chemical Physics, NIDDK, National Institutes of Health, 

Bethesda, M_D 20892. 

A number of modifications to existing 2D experiments are pr?po~d. 

Improvements in sensitivity and resolution of the ~H-detected ~H-~JC 

long range correlation (HMBC) experiment can be obtained by recording the 

spectrum in the absorption mode in the F, dimension and absolute value 

mode in F2. A recipe for non-interactive phasing of this and all other 

types of 2D spectra will be presented. 

A slightly different approach for suppressing zero quantum artefacts 

from NOESY spectra will be described and several mixing schemes for the 

HOHAHA/TOCSY experiment will be discussed and compared theoretically and 

experimentally. It is found that the optimal scheme depends on the 

electronics used for phase shifting, i.e., on the type of spectrometer 

used. 

36

10:40 a.m. 

11:00 a.m. 

11:20 a.m. 

11:30 a.m. 

11:40 a.m. 

12:10 p.m. 

TUESDAY MORNING 

SELECTIVE PULSE SEQUENCES 

A. Bax, Session Chair 

Composite Pulses: New Applications and Methods. 

T. Bielecki, *M. H. Levitt, 

J. L. Sudmeier, W. H. Bachovchin. 

Water Suppression Techniques for the Generation of Pure 

Phase NMR Spectra. 

V. Sklenar. 

Elimination of Phase Roll, Solvent Suppression, and Uniform 

Spin-1 Excitation with Shaped Pulses. 

W. S. Warren, M. McCoy, *A. Hasenfeld. 

Frequency Switched Inversion Pulses and Their Application 

to Broadband Decoupling. 

T. Fujiwara, *K. Nagayama. 

Fun with Genes. 

R. Freeman. 

Lunch. 

37

TUE 10"40 I 

COMPOSITE PULSES: NEW APPLICATIONS AND METHODS 

Tony Bielecki and Malcolm H. Levitt , 

Massachusetts Institute of Technology, Cambridge, MA 02139; 

James L. Sudmeier and William H. Bachovchin, 

Tufts University School of Medicine, Boston, MA 02111 

The application of composite pulses as solvent peak suppression 

sequences will be discussed. A combination of coherent averaging 

theory with numerical optimization allows one to find simple 

six-pulse sequences which hold the phase of excited signals almost 

constant, while cutting out a narrow, flat notch at the solvent 

resonance. This helps greatly to reduce distortions of the baseline 

and of broad or overlapping signals. Suppression ratios are not 

dramatic, but seem to be sufficient, especially in conjunction with 

an improved receiver design. 

It is also hoped to show results for composite pulses where the 

component pulses have different frequencies. New advances in direct 

digital frequency synthesis have made it feasible to achieve very 

fast jumps in carrier frequency, while maintaining phase coherence. 

This is expected to allow short but very broadband composite pulses, 

which will have implications in low-power population inversion and 

decouplinq experiment~. 

38

TUE ii'00 J 

WATER SUPPRESSION TECHNIQUES FOR THE GENERATION 

OF PURE PHASE NMR SPECTRA 

Vladimir Sklen~ 

Institute of Scientific Instruments, Czechoslovak 

Academy of Sciences, CS-612 64 BRNO, Czechoslovakia 

A large variety of selective excitation techniques are available 

for suppression of the intense H20 resonance in the NMR spectra 

of water soluble compounds. However, only a few methods yield spec- 

tra that are free of phase (and cosequently baseline) distorsions 

and can be applied in the pure absorption 2D NMR experiments. New 

class of two stage selective excitation techniques that offer very 

good water suppression, ideal phase profile and different amplitude 

profiles will be discussed. These methods use time shared hard pulse 

sequences or combinations of soft and hard pulses and take advan- 

tage of the phase cycling to achieve desired properties. Application 

to the measurement of pure phase 2D NMR spectra of small proteins 

and DNA fragments will be presented. 

39

TUE 11:20 

ELIMINATION OF PHASE ROLL, SOLVENT SUPPRESSION, AND UNIFORM SPIN-I 

EXCITATION WITH SHAPED PULSES: Warren S. Warren, Mark McCoy and 

Andy Hasenfeld*, Department of Chemistry, Princeton University, 


We have recently shown that purely amplitude modulated or phase/amplitude modu- 

lated pulses can eliminate phase roll while exciting regions as narrow as 15 Hz; can 

produce undistorted two-dimensional spectra off resonance while completely eliminating 

the solvent peak; and can excite a broader quadrupolar powder pattern for the same 

amplifier peak power. All of these experiments were done with a slightly modified 

commercial spectrometer. Theoeretical work has uncovered a new infinite family of 

pulses with a rectangular excitation profile and complete insensitivity to r.f. field 

strength (similar to the (sech(aT)) l+Di pulses demonstrated by Silver), but the 

additional degrees of freedom permit improved phase characteristics and give new 

insight into the effects of pulse shaping. 

References: 

M. McCoy and W.S. Warren, Chem. Phys. Lett. 133, 165 (1987). 

F. Loaiza, M. McCoy, S. Hammes and W.S. Warren, J. Mag. Res. (in press). 

A. Hasenfeld, Phys. Rev. Left. (submitted). 

40

TUE 11:30 J 

FREQUENCY SWITCHED INVERSION PULSES AND THEIR APPLICATION TO 

BROADBAND DECOUPLING; Toshimichi Fujiwara and Kuniaki Nagayama 

Biometrology Lab, JEOL Ltd. Nakagami, Akishima, Tokyo 196, Japan 

First, the broadband inversion pulses with coherent 

frequency switching were designed. They are made of a few 

180°-like pulses which are different in frequency of about 

1.5 x B , where B indicates strength of r.f. field. The 

refined frequency differences and pulse widths were numerically 

searched under the constraint of symmetry about offset frequency. 

The operative frequency range of these pulses is about 

1.2 x B x n, where n is the number of frequencies used, or the 

number of 180 ° pulses in the sequence. Second, its performance 

and the tolerance to inhomogeneity of B field were improved by 

the phase cycling of 0 ° , 150 ° , 60 ° , 150 ° , 0°. * Finally, 

decoupling pulse sequences were constructed from these improved 

inversion pulses using the phase cycle employed in MLEV-4. The 

performance of these pulse sequences was experimentally tested, 

and theoretically evaluated with two scaling factors; J-scaling 

factor which characterizes the decoupling on a long time scale 

(long period scaling) and a scaling factor which characterizes 

the decoupling on a short time (short period scaling). 

*R.Tycko, A. Pines, Chem. Phys. Letters iii, 462 (1984). 

41

TUE 11:40 

FUN WITH GENES: Ray Freeman, Cambridge University, 

] Cambridge CB2 IEP, England. 

If you are bored by endlessly searching For minlma in multidimensional 

hyperspace, why not try a new approach to the design of NMR pulse sequences? 

Now it is the scientist who makes all the important decisions while the 

computer merely calculates some figure of merit - for example a frequency-domain 

response function. The idea is not to optimlse an experiment but to discover 

new ones. Suppose we are interested in shaped selective radiofrequency pulses~ 

we might multiply a Gaussian by a sinc function or a polynomial and truncate 

the tails. Each contribution to the overall shape is assigned a "gene", a 

numerical value which can be incremented or decremented to represent a 

"mutation". fhe computer evaluates the frequency-domain excitation spectrum 

and displays it on an oscilloscope screen, together with its eight "offspring" 

obtained by changing one or two genes. If some "desirable" trend can be 

recognized, the operator selects that pattern as the parent for the next 

generation; if not he chooses arbitrarily or even recklessly, it doesn't 

matter. Eventually after several generations something new emerges. After 

all, that is how we all originated, through Darwinian natural selection. 

Ihis "genetic evolution" technique (I-3) is very general; it has been used in 

aeronautical engineering and in the automotive industry. It might just put the 

fun back into our own specialized 11ttle NMR games. 

(I) R. Dawkins, "The Blind Watchmaker", Longman 1986. 

(2) I. Rechenberg, "Evolutionsstra(e~ie'~ Frommann-Holtzboog, 1973 

(3) R. Freeman and X.L. Wu, J. Magn. Reson., 75, 18a (1987). 

42

7:30 p.m. 

8:00 p.m. 

8:30 p.m. 

8:50 p.m. 

TUESDAY EVENING 

HIGH Tc SUPERCONDUCTORS 

L. Jelinski, Session Chair 

Magnetic Resonance Studies of High Temperature 

Superconductors. 

C. P. Slichter. 

s3,6sCu NQR Studies of High Tc Oxide Superconductors. 

*W. W. Warren, R. E. Walstedt, 

G. F. Brennert, R. F. Bell, R. J. Cava, 

G. P. Espinosa, J. P. Remeika. 

Influence of High Temperature Superconductors on the 

Design of NMR Spectrometers. 

*H. Hill, G. Kneip. 

Cu NQR YBa2CuzOx with Varying Oxygen Content. 

*A. J. Vega, W. E. Farneth, 

R. K. Bordia, E. M. McCarron. 

43

I TUE Eve 7"301MAGNETIC RESONANCE STUDIES OF HIGH TEMPERATURE SUPERCONDUCTORS: 

Charles P. Slichter, University of Illinois at Champaign-Urbana, Urbana, IL 61801 

Nuclear spin-lattice relaxation times give important information about 

superconductors. The talk will briefly review the reasons. Then, it will turn to 

Cu NMR and NQR studies of powders of the 40 K superconductor Lal.85Ba.15CuO 4 and NMR 

studies of single crystals of the 90 K superconductor YBa2Cu307_ 6. 

Supported through the University of Illinois Materials Research Laboratory by the 

Department of Energy Division of Materials Research under Contract DE-AC01- 

76ERO1198. 

44

• . r 

T[-~-UE ~ t~ve 8:00! 63,65Cu NQR STUDIES OF HIGH T OXIDE SUPERCONDUCTORS: 

W. W. Warren, Jr.*, R. E. Walstedt, G. F. Brennert, R. F c. Bell, R. J. Cava, G. P. Espinosa, 

and J. P. Remeika, AT&T Bell Laboratories, Murray Hill, NJ 07974 

Nuclear quadrupole resonance provides a local, site selective probe which has proven highly 

informative for studies of oxide superconductors. In this talk I will review our investigations 

using the 6~,6SCu resonances in the 90 K superconductor YBa2Cu3OT_8" The crystal structure 

of YBa2Cu307 contains two inequivalent Cu sites (Cu-O ".chains" and "planes") whose NQR 

lines fall at roughly 22 MI-Iz and 31.5 MHz. Although electron band theory calculations imply 

similar electronic structure at the two sites, spin-lattice relaxation time measurements reveal 

strikingly different behavior in both the normal and superconducting states. In the normal 

states, the 22 MHz sites relax by an enhanced Korringa process that exhibits the usual roughly 

linear temperature dependence for the relaxation rate. At 31 MHz, in contrast, the rate 

increases only slightly with increasing temperature. Below To, spin-lattice relaxation reflects 

the excitation spectrum of unpaired electrons ("quasiparticles"). Again, the relaxation 

behavior is dramatically different for the two sites. An exponential representation of the 

relaxation rate yields a value 2A / kT c -- 2.4 for the 22 MI-Iz sites (A is the superconducting 

energy gap) while for 31.5 MHz, the corresponding value is 2A / kT c -- 8.3. Reduced oxygen 

content (8 = 0.3) leads to relaxation at the 31.5 MHz sites reduced by a factor - 1/1500 but 

only a modest 30 ~o effect at 22 MHz. This indicates that the former sites carry almost no 

conduction electron density and, by implication, do not participate in the 60 K 

superconductivity observed in this phase. The effects of extrinsic paramagnetic moments, the 

assignment of the NQR lines to the respective Cu sites, and the implications of these results of 

models of superconductivity will be discussed. 

45

TUE Eve 8" 30 I 

INFLUENCE OF HIGH TEMPERATURE SUPERCONDUCTORS ON THE DESIGN OF NMR 

SPECTROMETERS: Howard Hill* and George Kneip, Varian Associates, Palo 

Alto, CA 94303 

Recent discoveries of materials which are superconducting at liquid 

nitrogen temperatures raise the possibility of significant changes in the 

design and operation of NMR spectrometers. While the most obvious impact 

may be on the superconducting magnet itself and the associated cryogenics, 

there could also be major changes in the way in which the magnet and 

spectrometer are operated. In addition, the probe and rf electronics may 

also be enhanced by the use of superconducting components. 

A number of aspects of NMR spectrometer design will be discussed to 

indicate how performance and operation may be affected by further 

advances in superconducting technology. 

46

TUE Eve 8-50 } Cu NQR OF YBa2Cu30 x WITH VARYING OXYGEN CONTENT: 

A. J. Vega*, W. E. Farneth, R. K. Bordia, and E. M. McCarron, Central 

Research and Development Department, E. I. du Pont de Nemours and 

Company, Experimental Station, Wilmington, Delaware 19898~ 

The 63Cu and 65Cu NQR spectra of YBa2Cu30 x show a strong dependence 

on the oxygen content when x is varied from 6 to 7. For x=7 two 

signals are observed at room temperature. The room-temperature 

signals generally consist of a short-T 1 (< 1 ms) and a long-T 1 

component (~ 100 ms). The relative intensity of the short-T 1 

component gradually decreases from 100% to 0% when x is decreased 

from 7.0 to 6.0. In addition, the line shapes of the two T 1 

components are strongly dependent on the oxygen content. While the 

short Tl's are attributed to a Korringa-type relaxation mechanism 

involving the conduction electrons, it may be assumed that the Cu 

sites with the longer T 1 values are not directly associated with the 

conduction process. The NQR data can thus be used to help interpret 

the strong dependence of T c on the oxygen content of these 

superconducting materials. 

47

8:30 a.m. 

9:00 a.m. 

9:25 a.m. 

9:35 a.m. 

9:45 a.m. 

10:10 a.m. 

WEDNESDAY MORNING 

MATERIALS IMAGING 

A. Garroway, Session Chair 

Removal of Extraneous Line Broadening for Solid State 

Imaging: How Much Is Enough? 

J. B. Miller, *A. N. Garroway. 

New Imaging of Rigid Solids. 

D. G. Cory, A. Reichwein, J. Van Os, 

*W. So Veeman. 

A Static NMR Image of a Rotating Object. 

*S. Matsui, K. Sekihara, H. Shiono, 

H. Kohno. 

Solid State Back Projection Imaging. 

J. Listerud, *G. Drobny. 

Fluid and Solid State NMR Imaging Techniques for Studying 

the Processing of Advanced Ceramic Components. 

*J. L. Ackerman, L. Garrido, 

W. A. Ellingson, J. D. Weyand. 

Break. 

48

~X 

[I'IED 8:30 I 

REMOVAL OF EXTRANEOUS LINE BROADENING FOR SOLID STATE 

IMAGING: HOW MUCH IS ENOUGH, J. B. Miller and A. N. Garroway*, 

Naval Research Laboratory, Code 6122, Washington D. C. 20375-5000 

There are questions in materials science which can be 

addressed by NMR imaging. Under some circumstances, there is 

sufficient molecular motion within the specimen so that the now 

familiar techniques of medical NMR imaging (MRI) can be applied 

almost directly. However, the more general case requires methods 

specifically for imaging rigid solids. 

In this talk we present a number of solid state imaging 

approaches. Homonuclear line narrowing sequences are appended to 

the usual Fourier transform imaging procedure to produce two- 

dimensional images of solids. Even rare sDin imaging is tenable, 

as other workers have shown. Though the 13C signal is weaker 

than that of IH, heteronuclear decoupling is generally more 

efficient than homonuclear decoupling in organic polymers. But 

reducing only the dipolar contribution to the linewidth may not 

be sufficient for best spatial resolution. We demonstrate the 

removal of chemical shift-like broadening (isotropic and 

anisotropic chemical shifts, susceptibility, static field 

inhomogeneity) for both abundant (~H) and rare spin (13C) solid 

state imaging. We also present line narrowing methods and the 

first results for solid state imaging with a surface coil. 

49

h 

[WED 9-00 I 

NMR IMAGING OF RIGID SOLIDS 

l 

D.G. CORY, A. REICHWEIN, J.W.M. VAN OS, W.S. VEEMAN 

LABORATORY OF PHYSICAL CHEMISTRY 

UNIVERSITY OF NIJMEGEN 

6525 ED NIJMEGEN, NETHERLANDS 

IH NMR images of solids have been obtained by performing proton line narrowing 

(MREV-8 and ~S) concurrently with imaging. This combination of techniques allows 

a wide variety of imaging experiments. We employ a rotating magnetic field gradient 

synchronized to the spinning of the sample (1). Image reconstruction techniques are 

used by varying the phase difference between the gradient and the spinner. 

Distortion of images due to the distribution of isotropic chemical shift are 

eliminated by a numerical procedure in the time domain (2). The present resolution 

is ~ 30 ~lm. 

(I) D.G. Cory, J.W.M. van Os, W.S. Veeman; J.M.R. in press. 

D.G. Cory, A.M. Reichwein, J.W.M. van Os, W.S. Veeman; Chem. Phys Letters, 

in press. 

(2) D.G. Cory, A. Reichwein, W.S. Veeman; J.M.R., submitted. 

50 

(~)

. r 

WED 9:25 ] 

A STATIC NMR IMAGE OF A ROTATING OBJECT 

S. Matsui,* K. Sekihara, H. Shiono, and H. Kohno 

Central Research Laboratory, Hitachi, Ltd. 

P.O. Box 2, Kokubunji, Tokyo 185, Japan. 

An approach to imaging of a rotating object is described and demonstrated experimentally. 

The principle is to apply field gradients such that the N~ signal from the 

rotating object observed under the applied gradients results in appropriate scanning 

in the spatial frequency domain, or the k space. The scanning pattern must cover the 

k space as uniformly as possible. A static image of the rotating object can be obtained 

from such a scanning pattern by suitable data processing. 

When the whole object is moving, one must consider the field gradients in the 

moving object frame, G (t), (not in the laboratory frame, ~R(t)). Then, the signal 

scanning pattern in the object-frame k 

r 

space is 

(t) = W gr (t')dt' = Y 0 

r 

I 

Here, D_ is a transformation depending on the object motion. In the case of rotation 

about t~e Y axis at an angular frequency~o s, D G is given by 

(o t 0 

DG= 0 s 1 0 s 

t 0 cos ~ t . 

-sin ~s s 

In our preliminary two-dimensional (x,z) experiment, a gradient sequence in the 

laboratory frame, B~(t) = (Go~O t, 0, Go), was applied to obtain a spiral scanning 

K 

pattern in the object frame, k ~t) = (~G~tsin~ t, 0, Y G^tcos~ t). A phantom, 

r u V S 

consisting of two water-filled capillaries (~l.5Sand 2 nnn 1.d.), was rotated at 180 

Hz. The obtained proton image was consistent with the dimensions of the phantom. 

51

IWED 9:35 J 

SOLID STATE BACK PROJECTION IMAGING 

JOHN LISTERUD AND GARY DROBNY 

DEPARTMENTS OF ELECTRICAL ENGINEERING AND CHEMISTRY 

UNIVERSITY OF WASHINGTON, SEATTLE, WA 98195 

Abstract 

The requirements of an NMR imaging system dedicated to materials science will be 

quite distinct from those of medical imaging. Not the least of these differences will be the 

degree of flexibility demanded of a research laboratory system as compared to the turn- 

key philosophy of the clinical imager. In particular, the materials sciences challenge the 

spectroscopist to combine the classic NMR spectroscopies with the imaging experiment. 

To these ends we describe the construction of a multi-purpose microscopic NMR imaging 

probe for use on a standard spectrometer, and the efficient adaptation of standard two 

dimensional NMR data processing utility to image processing. The probe is capable of 

a variety of experiments, including the Kumar-Welti- Ernst experiment, backprojection 

by mechanical rotation of the sample, and backprojection by electronic rotation of gradi- 

ents. Because of its simplicity, backprojection promises to be especially straightforward 

to combine with spectroscopic techniques such as chemical shift and multiple quantum 

spectroscopy. Furthermore, "macro" feature of the standard two dimensional NMR data 

processing utility has a natural extension to tailored image processing, as demonstrated 

here by Tl and diffusion weighting of image grey scales. 

52

WED 9" 45 IFLUID AND SOLID STATE NMR IMAGING TECHNIQUES FOR STUDY- 

ING THE PROCESSING OF ADVANCED CERAMIC COMPONENTS: Jerome L. Ackerman, *~ 

Leoncio Garrido, ~ William A. Ellingson, b and John D. Weyand; ~ ~Department of Radiology, NMR 

Facility, Massachusetts General Hospital, Boston, MA 02114; bMaterials and Components Technol- 

ogy Division, Argonne National Laboratory, Argonne, IL 60439; CResearch Laboratory, ALCOA 

Technical Center, Alcoa Center, PA 15069 

Nuclear magnetic resonance imaging has had major impact on medical diagnosis, but has only 

recently been investigated for its potential as an analytical tool in the study of nonbiological ma- 

terials. Applying imaging techniques to, for example, a polymeric material offers the possibility of 

studying many of the physical and chemical properties normally analyzed with NMR, but now also 

in a manner which allows the determination of how these properties vary with position within the 

specimen. 

We have used both fluid-state and solid-state NMR imaging to study the processing of advanced 

ceramic materials. Elevated porosity or nonuniform binder distribution in green-state (unfired) 

specimens can lead to flaws in the final densified part, and subsequent failure in service. To image 

the porosity of a part, we introduce a carefully chosen tracer fluid into the specimen by vacuum 

impregnation. We define the NMR-derived porosity in a region as the fraction of maximum signal 

intensity normalized to that of pure tracer fluid. We image the polymeric binders (burned out during 

final sintering) of green-state specimens with adaptations of standard 2DFT spin-echo techniques, 

with the echo times TE reduced from the typical clinical range of 15 to 100 msec to the range of 

600 itsec to 4 msec, in correspondence to the T2's of these materials. We employ image processing 

'and display techniques to enhance the understandability of the image data, and to derive measures 

of t, niformity such as porosity distribution functions. 

53

10:30 a.m. 

11:00 a.m. 

11:10 a.m. 

11:35 a.m. 

11:45 a.m. 

12:10 p.m. 

WEDNESDAY MORNING 

BIOLOGICAL IMAGING 

R. A. Byrd, Session Chair 

Multivolume Selective Spectroscopy, Deuterium Imaging and 

lzC-NMR as Tools for the Study of 

in vivo Metabolism. 

*J. Seelig, S. Muller, J. Link, 

S. Cerdan. 

Human in vivo Spectroscopy at 4.0T. 

D. Hentschel, J. Vetter, R. Ladebeck, 

*M. J. Albright. 

Self Shielded Gradient Coils and Their Applications to 

Imaging. 

*P. B. Roemer, W. A. Edelstein, 

G. H. Glover. 

Quantification of Blood Flow and Tissue Perfusion via 

Deuterium NMR -- The Novel Use of D20 as a Freely 

Diffusible Tracer. 

*J. J. H. Ackerman, S. G. Kim, C. S. Ewy, 

N. N. Becker, Y. C. Hwang, R. A. Shalwitz. 

Angiography Using Magnetic Resonance. 

*A. Macovski, D. G. Nishimura. 

Lunch. 

54

i 

MULTIVOLUME SELECTIVE SPECTROSCOPY, DEUTERIUM IMAGING AND. 13C-NMR 

~ED 10:30 I AS TOOLS FOR THE STUDY OF IN VIVO METABOLISM 

Joachim Seelig , S. MUller, J. Link, and S. Cerdan, Biocenter, University of Basel, 

Basel, Switzerland 

The main problem of in vivo spectroscopy is the precise selection of the region of 

interest with sufficient sensitivity. Image-guided, simultaneous sgectroscopy of 

multiple volumes is possible via the application of frequency selective pulses 

31 

composed of several excitation frequencies. The feasibility of multivolume P-NMR 

spectroscopy will be demonstrated for phantoms and for human heart. The availability 

of a rampable magnet allows routine MR-Imaging at 1.5 T and MR-Spectroscopy at 2 T 

with only 20 min intervals. Deuterium MR-Imaging will be introduced as a new method 

for contrast enhancement and flow. The application of 13C-NMR to the in vivo study 

of liver metabolism of rat will be discussed. 

55

WED ii:00 J 

HUMAN IN VIVO SPECTROSCOPY AT 4.0T 

Dietmar Hentschel, Jurgen Vetter, Ralf Ladebeck, and Michael J. Albright* 

Siemens AG, D-8520 Erlangen, FDG 

A 4 T six-coil SCM with a warm bore of 1.25 m diameter was designed 

with high homogeneity for use with in vivo spectroscopy. Computer optimized 

design was used to correct terms up to 10th order. The magnet can be ramped 

to 4 T in 1 hour. The rated current is 376 A, and the stored field energy is 39 

MJ. The field drift is less than 3.6 x 10-e/h, and bare homogeneity of 100 ppm 

can be corrected to less than +2.5 ppm for a 50 cm dsv. The total magnet 

weight is 10.6 tons. 

Increased spectral dispersion will be shown by comparison with 2 T 

spectra. Human in vivo 31p spectra at 4 T show resolution of the different 

PDE resonances, and, on some spectra, separation of the dinucleotides and 

nucleoside diphosphosugars upfield of the (z-ATP peak. 

High field RF penetration will be demonstrated with a 1H image at 4 T. 

56

[WED 11-10 I SELF SHIELDED GRADIENT COILS AND THEIR APPLICATIONS 

TO IMAGING: P. B. Roemer *1, W. A. Edelstein 1, G. H. Glover 2. (1) GE Corporate Research and 

Development Center, Schenectady, NY 12345. (2) GE Medical Systems, Milwaukee, WI 53188. 

Gradient induced eddy currents adversely affect many imaging and volume spectroscopy techniques. In this 

talk we cover three aspects of gradient coil design and their applications: i) the nature of gradient induced 

eddy currents and their correctable and uncorretable components; ii) the design of self-shielded gradient coils 

and limits to which they can reduce eddy currents; iii) the impact of eddy currents on imaging and selective 

volume spectroscopy experiments. 

We show that unshielded gradient coils of conventional design produce eddy currents on the order of 20% 

of the gradient field. Shaping of the gradient waveform is typically used to compensate for eddy currents and 

this technique in general can only be used to correct a single point in space. Other points in the imaging 

volume will have time dependent field errors on the order of a few tenths of a percent. We show that this 

level of eddy currents can adversely affect many imaging experiments such as multi-echo multi-slice, cardiac 

cine, phase contrast angiogrophy and volume selective spectroscopy. By using self-shielded gradient coils it 

is readily possible to reduce eddy currents by at least another factor of 30, making them almost undetectable. 

Results are presented for coils we have designed and operated that range from small fast gradients (20 G/cm 

100 usec risetime, 15 cm bore) operated in small bore imaging systems to whole body imaging gradients 

(1G/cm, 500 usec, 66 cm bore). 

57

Wed 11:55 

QUANTIFICATION OF BLOOD FLOW AND TISSUE PERFUSION VIA DEUTERIUM 

I NMR-THE NOVEL USE OF D=O AS A FREELY DIFFUSIBLE TRACER: 

Joseph J.H. Ackerman i W , Seong-Ci Kim*, Coleen S. Ewy*, Nancy N. 

56cker*, Yuying C. Hwang*, and Robert A. Shalwitz2; Departments of Chemistry* and 

Pediatrics 2, Washington University, St. Louis, MO 631301 and 631102 . 

NMR has proven to be a valuable technique with which to monitor metabolic events 

nondestructively in intact biological systems. The past decade has witnessed dramatic 

advances in the development of such spectroscopic analyses employing alp, 13C, and *H 

nuclides. Our laboratory has recently introduced a new approach, employing deuterium 

NMR in concert with D20 as a freely diffusible aqueous tracer, for the measurement of 

blood flow and tissue perfusion I'2 This method borrows heavily from multicompart- 

ment kinetic modeling used with diffusible radiotracers such as H2*SO and 133Xe but,of 

course, does not require the special handling procedures associated with radioactive 

labels. In addition, the deuterium NMR blood flow determination can be carried out 

concomitant with NMR metabolic analysis, thus, correlating in one measurement impaired 

substrate delivery and its physiologic consequences. In brief, the tissue or organ in 

which blood flow is to be determined is labeled with D20 via either intravenous, intra 

arterial or intratissue bolus injection. Ongoing capillary blood flow, diffusion and 

proton-deuteron exchange serve to distribute HOD throughout the tissue's aqueous space 

Further blood flow (unlabeled) then washes out the deuterium residue. The residue 

decay (washout) curve is accurately defined via external monitoring, i.e., 2H NMR. 

Single*, ~ and multicompartment modeling 3'4 and knowledge of the blood:tissue 

partition coefficient (readily determined independently of the NMR residue decay curve 

allows derivation of blood flow and perfusion in units of ml-blood/(lO0 g-tissue,min). 

The extension of this method to NMR flow-imaging appears feasible s . [References: (i) 

J.J.H. Ackerman et al., Proc. Natl. Acad. Sci. USA, 84, 4099 (1987); (2) J.J.H. 

Ackerman et al., N.Y. Acad. Sci., 508, 89 (1987); (3) S.-G. Kim et al., Cancer 

Research, accepted (1987); (4) S.-G. Kim, et al., Magn. Reson..Med., submitted 

(1987); (5) C.S. Ewy eC al., Magn. Reson. Med., submitted (1987).] 

58

[WED 11:45 ] ANGIOGRAPHY USING MAGNETIC RESONANCE, Albert 

Nishimura, Dept. of EE, Stanford University, Stanford CA 94305 

Macovski~ and Dwight G 

Vessel disease is the number one killer of western man, with coronary artery lesions 

the principal source of heart disease, and carotid artery lesions the principal source 

of strokes. We will present an array of techniques for studying these vessels with 

magnetic resonance imaging, a completely non-invasive procedure. Each of the approaches 

involves one or more combinations of three basic techniques: Phase shift in the pres- 

ence of a gradient, wash-in wash-out effects, or cancellation excitation. The first is 

a classical phenomenon whereby moving material acquires a phase shift proportional to 

the velocity component in the gradient direction. Systems have been developed which 

subtract the signals from two sequences having differing first gradient moments, thus 

displaying solely the moving material. The second approach involves an upstream excita- 

tion followed by a downstream readout, or a variety of similar approaches. We have been 

~articularly successful with an approach where the source of blood is subjected to an 

Lnversion excitation on one sequence and left unexcited on the next. When these are 

subtracted, using identical readout sequences, all static tissue cancels while the 

vessels are clearly visualized due to the large difference between the inverted and 

fresh spins. The third approach involves excitations which provide a net excitation for 

moving material only, while statlc material is left unexcited using a form of driven 

equilibrium. These vessel images are structured as projections through the volume of 

interest so that the entire vessel is visualized despite its tortuous path. One of 

the major problems is the phase shift produced by higher order moments, such as accel- 

eration due to turbulence. This can cause loss of signal in regions of narrowing, often 

I crucial portion of the image. Imaging sequences can be designed to make the readout 

ery close to the excitation, minimizing this problem. 

I 

59

8:30 a.m. 

8:55 a.m. 

9:20 a.m. 

9:30 a.m. 

9:40 a.m. 

10:05 a.m. 

THURSDAY MORNING 

ORDERED BIOLOGICAL SYSTEMS 

L. Batchelder, Session Chair 

"Tethered" Biological Systems: Results from NMR 

Spectroscopy. 

*L. Jelinski, R. W. Behling, D. Live, 

T. Yamane. 

Multinuclear Experiments for the Determination of Oligo- 

saccharide Structure in Liquid Crystal Phases. 

*J. H. Prestegard, P. Ram, 

L. T. Mazzola. 

Dynamics of the Gramicidin A Transmembrane Channel by 

Solid State lSN NMR. 

L. K. Nicholson, M. T. Brenneman, 

P. V. Lograsso, *T. A. Cross. 

Natural Abundance 13C and 14N NMR of Bacterial Osmolytes 

in vivo. 

*B. A. Lewis, S. C. Cayley, 

S. Padmanabhan, M. T. Record. 

NMR Studies of Anti-Spin Label Monoclonal Antibodies. 

*G. S. Rule, H. M. McConnell. 

Break. 

60

THU 8:30 "TETHERED" BIOLOGICAL SYSTEMS: RESULTS FROM NMR SPECTROSCOPY 

Lynn W. Jelinski," Ronald W. Behling, David Live, + and Tetsuo Yamane, AT&T Bell Laboratories, Murray Hill, NJ 07974. 

By "tethered" biological systems, we mean assemblies in which two or more molecules arc either covalently or transiently 

joined together for the purpose of biological action. Tethered systems are a recurring theme in biophysics; examples include 

enzyme - subswate complexes, DNA - protein interactions, receptor - ligand binding, and antigen - antibody recognition. 

NMR spectroscopy is exceptionally well-suited to address key questions regarding both site - site recognition and chain 

folding in tethere.d biological assemblies. 

We will briefly describe three examples of tethered assemblies. In the first, polymer - peptide hybrids were constructed of 

polystyrene onto which was grown oligoglycines with varying but monodisperse chain lengths. Using solid state deuterium 

NMR spectroscopy, we showed that peptidc - peptide association occurred when the chain lengths were sufficient to form one 

overlap of the polyglycine II triple helical repeat. 

In another example, high resolution proton NMR was used to study the binding of small ligands to the acetylcholine receptor. 

Once the strategy was in place for observation of binding by NMR, 2D-NOE experiments were performed to determine the 

conformation of acetylcholine in its receptor-bound state. The results show that the conformation of the receptor in the 

bound state is significantly different from that when free in solution, suggesting that structure-activity relationships based 

solely on X-ray or solution conformations must be approached with caution. 

We are presently attempting to answer the question of whether nucleation sites for protein folding are formed during protein 

synthesis. To answer this question, we are preparing "fake" ribosomes (polyacrylamide) onto which the initial peptide 

segments of the S-peptide of ribonuclease are attached. These "fake" ribosomes are designed to mimic the way in which a 

protein would be synthesized in the cell. These tethered structures will be compared to the NMR spectra of the S-peptide, 

whose solution state conformation is being determined. 

Taken together, our results suggest that a combination of modem NMR techniques and cleverly chosen systems will have a 

substantial impact on our understanding of the structure and function of complex hybrid biological systems. 

+ Department of Chemistry, Emery University, Atlanta, GA 30322 

61

THU 8:55 ] 

MULTINUCLEAR EXPERIMENTS FOR THE DETERMINATION OF 

OLIGOSACCHARIDE STRUCTURE IN LIQUID CRYSTAL PHASES: J. H. Prestegard~, 

Preetha Ram, and L. T. Mazzola, Department of Chemistry, Yale University, 

New Haven, CT 06511. 

The dependence of quadrupole and magnetic dipole splittings on orientation 

of internuclear vectors relative to applied magnetic fields can, in 

principle, provide a great deal of information on the conformation and 

orientation of molecules in llquld crystal phases. In practice, however, 

it is difficult to obtain a sufficient number of independent spllttlngs to 

reduce the ambiguity inherent in the multlvalued solutions for spllttlngs 

in terms of angles, and to eliminate order parameters which scale 

spllttlngs in these environments. 

We will show that in some cases, it is possible to obtain sufficient 

information by combining data from 2H quadrupole spllttlngs, 13C-IH dipolar 

spllttlngs, and IH-IH dipolar spllttlngs. Observation of these spllttlngs 

is facilitated by use of liquid crystal phases which are relatively free of 

background signals, and use of experiments which exploit unique 

spectroscopic properties of quadrupole and dipole couplings. In other 

cases, spectroscopic information can be supplemented with energetic 

descriptions of molecular conformations contained in molecular mechanics 

and molecular dynamics programs. Examples of structure determination on 

surface associated dlsaccharides and membrane anchored glycoltpids will be 

given. 

82

• / I 

DYNAMICS OF THE GRAMICIDIN A TRANSMEMBRANE CHANNEL BY 

THU 9:20 I SOLID STATE 15N NMR: L.I~ Nicholson, M. T. Brenneman, P.V. LoGrasso and 

T.A. Cross, Florida State University, Institute of Molecular Biophysics and 

Department of Chemistry, Tallahassee, Florida 32306. 

The dynamics of specific sites in the peptide backbone of the gramicidin A cation selective 

transmembrane channel have been studied using solid state 15 N NMR. Gramicidin A is a polypeptide 

consisting of fifteen amio acids which dimerizes to form a single stranded helical pore in a lipid bilayer. 

Its generally accepted structure is the ~6.3 helix which, due to the uniquely alternating L/D amino acid 

sequence places the bydrophobic side chains on the outside of the channel where they interact with the 

hydrocarbon core of the bilayer, and the polar peptide linkages along the interior of the channel which 

enhances solvation of the channel ion. Although gramicidin is the most extensively studied channel, an 

atomic resolution mechanism Of ion transport is not known. Characterization of motions of various groups 

within the channel backbone will help to elucidate the specific interactions that result in transport of the ion 

across the membrane. Motions of specific sites along the channel backbone have been detected by observing 

the averaging of the 15N chemical shift anisotropy (CSA) tensor as a function of temperature in both oriented 

and unoriented samples. It has previously been shown that fast overall channel rotation occurs in and 

above the lipid phase transition region, and that the axis of rotation coincides with the channel axis which is 

parallel to the bilayer normal. This global rotation becomes slow on the 3kHz timeframe of the NMR 

experiment when the temperature is below the onset of the phase transition. Recent studies of the temperature 

dependence of the 15N spectra of both oriented and unoriented samples show evidence for local motions of the 

peptide linkages existing above the onset of the gel to liquid crystalline phase transition, and that the 

amplitude of these motions varies along the channel backbone. These local motions have a large amplitude 

at the monomoer - monomer juction where the peptide linkage planes contribute a proton to the hydrogen 

bonds linking the two monomers. The temperature dependence of oriented samples where yield a very 

sharp resonance above the phase transition region has proved to be a very sensitive indicator of dynamics 

when the temperature is lowered. The resonance linewidth below the phase transition reflects directly on the 

range of orientations swept out by the dynamic process at higher temperatures. This new tool for assessing 

dynamics should have broad application in systems that can be oriented. 

63

I NATURAL ABUNDANCE 13 C and 14 N NMR (IF BACTERIAL OSIIOLYIES IN VlYO. B.A. 

THU 9 • 3 0 .I Lewis,eS.C.Cayley, S. Padmanabhan, and II.T. Record, dr. Dept. of Chemistry, 

University of Wisconsin, Madison Wl 53706. 

Bacteria such as E. Coil and_5, lyphimurium are capable ol growir 0 under conditions of moderately 

high osmotic stress, up to about 0.7 molar salt. To adapt to such hi~h-osmolarity enviror~ments, the b~~l.erial 

cell accumulates potassium ions and also synthesizes or accurnulal.es one or more small orgonic molecules. 

These include the anion glutamate and the neutral or zwitterionic molec..ules prol ine, glycine betaine (I,I,I,I,H- 

trimethyl glycine) and/or trehalase, a glucose dimer. Because these small molecules are accumulated to 

intracellular concentrations on the order of 0.5 molal, they are re~Jily observed in dense cell slurries by 

natural abundance 13 C NMR on our Bruker AM360 with a I 0 turn br-c,~lband probe. I '-1N NI'IR is al~ u.~ful to 

observe glycine betaine, which h~ a relatively narrow 14 N spectrum due to the symmetric environment of 

the nitrogen and its lack of exchangeable protons. 

We are able to measure the relative and absolute amounts of the various or~nic osmolytes ~..~:umulaled 

by the bacteria in vivo under a variety of environmental conditions. In minimal medium with 0.5 M l'laCI, 

trehalose and glutamate are the on!y small organic molecules pre~nt in high amounts. If I mM proline is added 

to the medium, it is accumulated to nearly 0.4 M intracellular ly, with some diminution of the trehsl~-e., and 

glutamate levels. Glycine betaine, however, also supplied at I raM, is accumulated to about 0.5 M, and 

trehalose is completely eliminated. 

Under these, high salt conditions, significant amounts of rf power are absorbed by the sample, 

particularly at the high frequencies of 90 IiHz for 13 C and 360 for i H. Thus for- the 13 C e×periments we 

employ gated proton decoupling to minimize sample heating. In ~.klition, the pulse lengths must be calibrated 

for each sample, and internal standards must be used for quantitative measurement. 

64

I THU 9:40 I 

NMR STUDIES OF ANTI-SPIN LABEL MONOCLONAL ANTIBODIES: D. J. Leahy, G. S. Rule', 

and H. M. McConnell, Dept. of Chemistry, Stanford University, Stanford, CA, 94305. 

Current progress towards the application of NMR to the study of proteins has been largely 

restricted to protein molecules of low (10-15 KDa) molecular weight. We are currently utilizing 

a number of approaches to obtain interpretable proton NMR spectra from a large protein, the Fab 

fragment of an immunoglobulin. 

The NMR spectra are simplified by methods of deuteration. We deuterate the Fab fragment 

With both perdeuterated and partially deuterated amino acids. The partial deuteration results in the 

removal of J coupling between protons. Thus we can observe and study individual resonance lines 

from aromatic protons of Tyr and Trp residues, and the methyl groups of Val, Leu, lie, Thr, or Ala 

residues. 

The proton NMR spectra are further simplified by utilizing a spin-labelled hapten to 

selectively broaden NMR signals from protons near the combining site. Chemical exchange of the 

hapten modulates this broadening effect and spectra obtained at different occupancy levels can yield 

measurements of the distance between the hapten and the amino acid residues in the range of 8-17 

A. 

By combining distance measurements, resonance assignments, and molecular modelling we 

intend to develop a working model of the antibody combining site. 

65

10:25 a.m. 

10:55 a.m. 

11:05 a.m. 

11:35 a.m. 

THURSDAY MORNING 

DYNAMIC NUCLEAR POLARIZATION 

N. Zumbulyadis, Session Chair 

New Techniques for Dynamic Nuclear Polarization. 

W. Th. Wenckebach. 

Time Domain ENDOR Studies of Disordered Solids. 

P. J. Tindall, M. Bernardo, 

*H. Thomann. 

Dynamic Nuclear Polarization: A Method for Surface- 

Selective NMR. 

*G. G. Maresch, R. D. Kendrick, 

C. S. Yannoni, M. E. Galvin. 

Dynamic Nuclear Polarization in the Nuclear Rotating Frame. 

*R. A. Wind, H. Lock, L. Li, 

G. E. Maciel. 

66

THU 10"2S I 

NEW TECHNIQUES POR 

DYNAMIC NUCLEAR POLARIZATION 

W.Th. WENCKEBACH 

KAMERLINGH ONNES LABORATORY, P.O.BOX 9506, 

2300 RA LEIDEN, THE NETHERLANDS 

Two new techniques for dynamic nuclear polarization have recently been 

developed: Microwave induced optical nuclear polarization (MIONP) and 

nuclear orientation via electron spin lock (NOVEL). In the first technique 

photoexcited states with an electron spin are used to polarize nuclear spins. 

As in classical dynamic nuclear polarization the electron spin polarization 

k transferred to the nuclear spins using cw microwave irradiation. In the 

second technique the electron spin polarization is transferred by means of 

pulsed microwave techniquea First the electron spin is locked by a ~-pulse 

followed by a ~--phase shift. Then the nuclear spins and the electron spins 

are brought to mutual resonance by choosing the Rabi frequency of the 

latter equal to Larmor frequency of the former. As a result polarization 

tr-~uffer ~ obee~ed. 

67

ITHU 10"55 I TIME DOMAIN ENDOR STUDIES OF DISORDERED SOLIDS: P. J. Tindall, M. 

Bernardo, and H. Thomann, EXXON Corporate Research Laboratory, Route 22 East, 

Annandale, N. J. 08801 

Spectral simplification, resolution enhancement, and sensitivity enhancement are well 

known advantages of multiple frequency techniques used in NMR. The ability to 

coherently excite and coherently transfer longitudinal or transverse magnetization 

among sub-levels of the spin system elgenstates is fundamental for the success of 

most of these experiments and is only possible with time domain pulsed excitation. Ir 

contrast to NMR, the most widely applied multiple resonance technique in ESR, the 

ENDOR experiment, has traditionally been performed in the frequency domain. However, 

recent advances in instrumentation have now made time domain ENDOR more feasible. 

The time domain analog of the CW-ENDOR exper-lment is magnetization transfer (MT) 

ENDOR using the Davies pulse sequence. MT-ENDOR has the advantage that the ENDOR 

enhancement does not depend on the ratio of the electron and nuclear T 1 rates as it 

does in CW-ENDOR. Furthermore, time domain excitation also makes possible more 

complex double resonance experiments which depend on coherence transfer, such as 

CT-ENDOR and splnor ENDOR recently demonstrated by Mehring et al. The general 

applicability of these techniques to disordered solids will be governed by electron 

T I and T m (phase memory) times which are typically shortened by disorder effects. 

Fortunately, in many cases of interest, relaxation times for hydrocarbon radicals in 

condensed hydrocarbons are sufficiently long for successful magnetization and 

coherence transfer experiments even at room temperature. Experiments on transition 

metal ion complexes and metal clusters are possible at liquid He temperatures. Some 

recent time domain ENDOR results on isolated coal macerals, polyacetylene, and frozer 

solutions of transition metal ion complexes will be presented. 

68

I THU 11 : 05 I 

DYNAMIC NUCLEAR POLARIZATION: A METHOD FOR SURFACE-SELECTIVE NMR 

G. G. Maresch, R. D. Kendrick, and C. S. Yannoni* 

IBM Research Division, Almaden Research Center, San Jose, California 

and 

M. E. Galvin 

AT&T Bell Laboratories, Murray Hill, New Jersey 

Dynamic Nuclear Polarization (DNP) holds promise as a method for the study of molecules 

at the surface of materials which contain unpaired electrons. The idea in the kind of 

experiments that will be described here is to use bulk samples, but to selectively polarize 

nuclei in molecules that sit on the Internal surfaces of "islands" of electron-rich material 

that has been dispersed in the bulk. Selectivity is achieved via the short range of the 

electron-nuclear coupling. The bulk material may be an organic or inorganic solid or 

polymer (e.g. polyethylene), while the electrons may be localized in metal clusters or 

small islands of a semiconductor like polyacetylene. The requirement of confining the 

dynamic polarization of even rare nuclei like 13C to the surface of the electron-rich islands 

poses a challenge and our efforts to do this have resulted in the confirmation of a 

"three-spin" effect. Although related observations have been made in DNP studies of 

dilute solutions of free radicals 1, the three-spin effect discussed here arises from a 

number of dynamical processes peculiar to the static configuration of the three spins 

(electron, proton and carbon in this case) in solids. 

. R. E. Richards and J. W. White, Disc. Faraday Soc. 3._44, 96 (1962); 

K. H. Hausser and F. Reinbold, Phys. Lett. 2 , 53 (1962). 

69

THU 11:35 I 

DYNAMIC NUCLEAR POLARIZATION IN THE NUCLEAR ROTATING FRAME, R~A. 

Wind, H. Lock, L. Li and G.E. Maciel, Department of Chemistry, 

Colorado State University, Ft. Collins, CO 80523. 

Traditionally Dynamic Nuclear Polarization (DNP) has been used to enhance the 

nuclear polarization directed along the external magnetic field. Several DNP mecha- 

nisms can be responsible for this polarization enhancement, depending on the time- 

dependence and character of the electron-nuclear interactions: the Overhauser 

effect, the Solid-state effect and the direct and indirect thermal mixing effects. 

In solids containing organic radicals all mechanisms often determine the observed 

enhancement. It will be shown that it is also possible to enhance the nuclear 

polarization in its rotating frame. This is obtained by irradiating with a strong 

r.f. field at the nuclear Larmor frequency during the microwave irradiation. Com- 

pared with the conventional method of DNP this technique has several advantages: 

(i) the build-up time of the nuclear polarization is determined by the rotating- 

frame relaxation time, which is often much shorter than the Zeeman relaxation time; 

(ii) The 'forbidden' transition rate, which determines the enhancement due to the 

indirect thermal mixing effect, is several orders ofmagnitude larger in the rotating 

frame than in the laboratory frame. As a result the enhancement due to this effect 

is one to two orders of magnitude larger in the rotating frame than in the labora- 

tory frame; (iii) If the Zeeman relaxation time is short, the DNP enhancement in the 

laboratory frame can be reduced, whereas the rotating-frame enhancement remains 

large; (iv) rotating-frame DNP of abundant spins opens the possibility for multiple- 

contact cross-polarization (CP) experiments and for CP experiments with long contact 

times, independent of the value of the rotating-frame relaxation time. 

Applications will be shown of rotating-frame 1H DNP and 13C-1H CP experiments 

in doped styrene and coal. 

70

THIS SECTION CONTAINS A LISTING OF POSTERS 

FOLLOWED BY THE ABSTRACTS IN THE SAME SEQUENCE 

AS THE LISTING. 

PLEASE NOTE THE NUMBER PRECEDING EACH TITLE 

IN THE LISTING. EACH POSTER SHOULD BE MOUNTED 

ON THE BOARD WITH THE CORRESPONDING NUMBER. 

AUTHORS OF POSTERS WITH EVEN NUMBERS SHOULD BE 

PRESENT DURING THE POSTER SESSION ON MONDAY AFTERNOON. 

AUTHORS OF POSTERS WITH ODD NUMBERS SHOULD BE 

PRESENT DURING THE WEDNESDAY AFTERNOON SESSION. 

71

1 SOLID PHASE CARBON-13 NMR STUDIES OF CROWN ETHERS AND THEIR 

COMPLEXES; *BUCHANAN, G W, MORAT, C, KIRBY, R A, RATCLIFFE, C I 

AND RIPMEESTER, J A; CARLETON UNIV, OTTAWA, CANADA. 

2 A NEW APPROACH FOR QUANTITATIVE 13C-NMR SPECTROSCOPY OF COAL; 

*BOTTO, R E, MUNTEAN, J V AND STOCK, L M; ARGONNE NAT'L 

LABORATORY, ARGONNE, IL. 

3 31P SOLID STATE NMR STUDIES OF ZrP, Mg3P2, MgP4, AND CdPS3; 

*NIISAN, R A AND VANDERAH, T A; NAVAL WEAPONS CTR, CHINA LAKE, 

CA. 

4 HIGH RESOLUTION SPECTRA OF LIQUIDS IN INHOMOGENEOUS 

ENVIRONMENTS AS ONTAINED BY MASS; *RUTAR, V; IOWA STATE UNIV, 

AMES, IA. 

5 CONSTRAINED DECONVOLUTION OF 2D NMR SPECTRA AND IMAGES; 

*SOLE, P, DELAGLIO, F AND LEVY, G C; NEW METHODS RESEARCH, 

SYRACUSE, NY. 

6 AUTOMATED HI SPECTRA MADE ON AN XL-300; 

UPjOHN CO, KALAMAZOO, MI. 

*SLOMP, G; THE 

7 CALCULATION OF 29SI MAS NMR CHEMICAL SHIFT FROM SILICATE 

MINERAL STRUCTURE; *SHERRIFF, B L AND GRUNDY, H D; MCMASTER 

UNIV, HAMILTON, CANADA. 

8 NONLINEAR INCOHERENT SPECTROSCOPY; PAFF, J AND *BLUMICH, B; 

MAX-PLANCK-INST F POLYMERFORSCHUNG, MAINZ, FRG. 

72

9 ELIMINATION OF PHASE ROLL, SOLVENT SUPPRESSION, AND 

UNIFORM SPIN-1 EXCITATION WITH SHAPED PULSES; WARREN, W S, 

MCCOY, M AND *HASENFELD, A; PRINCETON UNIV, PRINCETON, NJ. 

10 127I NMR STUDY OF QUADRUPOLAR ECHOES IN KI; 

C; MCGILL UNIV, MONTREAL, CANADA. 

*SANCTUARY, B 

11 AN NMR STUDY OF MISCIBLE BLENDS IN CONCENTRATED SOLUTION; 

*CROWTHER, M W, CABASSO, I AND LEVY, G C; NEW METHODS RESEARCH, 

SYRACUSE, NY. 

12 POTENCY OF FLUORINATED ETHER ANESTHETICS CORRELATES WITH 

SPIN-SPIN RELAXATION TIME IN BRAIN; *D'AVIGNON, D A, HAYCOCK, J 

C AND EVERS, A S; WASHINGTON, UNIV, ST LOUIS, MO. 

13 QUANTIFICATION OF BLOOD FLOW AND TISSUE PERFUSION VIA 

DEUTERIUM NMR - THE NOVEL USE OF D20 AS A FREELY DIFFUSIBLE 

TRACER; *ACKERMAN, J J H, KIM, S-G, EWY, C S, BECKER, N N, 

HWANG, Y C AND SHALWITZ, R A; WASHINGTON UNIV, ST LOUIS, MO. 

14 SILICON-29 MASNMR ANALYSIS OF SINTERED Si3N4 CERAMICS; 

*CARDUNER, K R; FORD MOTOR CO, DEARBORN, MI. 

15 19F CRAMPS OF INORGANIC FLUORIDE COMPOUNDS; *SMITH, K A 

AND BURUM, D P; COLGATE-PALMOLIVE, PISCATAWAY, NJ. 

16 13C NMR RELAXATION STUDIES OF GLUCONATE AND MANCANESE- 

GLUCONATE INTERACTIONS~ *CARPER, W R AND COFFIN, D B; WICHITA 

STATE UNIV, WICHITA, KS. 

73

17 QUANTITATIVE 2D NMR STUDIES OF PROTON EXCHANGE IN AMMONIUM 

ION; *PERRIN, C L AND DWYER, T J; UNIV OF CALIFORNIA, SAN 

DIEGO, CA. 

18 TWO-DIMENSIONAL NMR STUDIES OF THE CONFORMATIONS OF 

BRADYKININ IN AQUEOUS SOLUTION AND IN THE PRESENCE OF MICELLES; 

*LEE, S C AND RUSSELL, A F; PROCTER & GAMBLE, CINCINNATI, OH. 

19 DIPOLAR AND SPIN-ROTATION POLARIZATION OF METHYL GROUP 

SPINS; *MURPHY, M AND WHITE, D; UNIV OF PENNSYLVANIA, 

PHILADELPHIA, PA. 

20 NMR SIGNAL PROCESSING USING PADE APPROXIMANT AND LINEAR 

PREDICTION Z-TRANSFORM METHOD; *TANG, J, ZENG, Y AND NORRIS, J 

R; ARGONNE NAT'L LABORATORY, ARGONNE, IL. 

21 24 DETECTION OF LONG-RANGE 1H-19F COUPLINGS USING A 

HETERONUCLEAR EQUIVALENT OF THE COSY PULSE SEQUENCE; *HUGHES D 

W AND BAIN, A D; MCMASTER UNIV, HAMILTON, CANADA. 

22 STUDIES OF PHOSPHORYLATED SITES IN PROTEINS USING 1H-31p 2- 

DIMENSIONAL NMR; *LIVE, D H AND EDMONDSON, D E; EMORY UNIV, 

ATLANTA, GA. 

23 A SOLID-STATE 2H AND 13C NMR STUDY OF THE STRUCTURE OF 

POLYANILINES; *KAPLAN, S, CONWELL, E M, RICHTER, A F AND 

MACDIARMID, A G; UNIV OF PENNSYLVANIA, PHILADELPHIA, PA. 

24 TWO-DIMENSIONAL FLUORINE NMR; 

UNIV OF FLORIDA, GAINESVILLE, FL. 

74 

*PLANT, H D AND BREY, W S;

25 NUCLEAR MAGNETIC RESONANCE STUDIES OF GROUP VI METAL 

CARBONYLS ON OXIDE SUPPORTS; *SHIRLEY, W M; WICHITA STATE UNIV, 

WICHITA, KS. 

26 A NOVEL METHOD FOR DETERMINING ACTIVATION ENERGIES AND 

CORRELATION TIMES FROM NMR SPIN-LATTICE RELAXATION DATA; 

*FINEMAN, M A; SAN DIEGO STATE UNIV, SAN DIEGO, CA. 

27 COLLECTION OF PHOSPHORUS-31NMR SPECTRA FROM RAT PUPS WITH 

INDUCED HYPERTHERMIA; *FORD, J J, TABER, K H AND BRYAN, R N; 

BAYLOR MAGNETIC RESONANCE CTR, HOUSTON, TX. 

28 HIGH PRESSURE DEUTERIUM SOLID STATE NMR OF POLYCRYSTALLINE 

CdPS3 INTERCALATED WITH PYRIDINE; *MCDANIEL, P L, LIU, G AND 

JONAS, J; UNIV OF ILLINOIS, URBANA, IL. 

29 SOLID-STATE NMR STUDY OF THE STRUCTURE AND DYNAMICS OF 

PLANT POLYESTERS AND INTACT PLANT CUTICLE; *GARBOW, J R 

ZLOTNIK-MAZORI, T, FERRANTELLO, L M AND STARK, R E; MONSANTO CO, 

ST LOUIS, MO. 

30 A STATIC NMR IMAGE OF A ROTATING OBJECT; *MATSUI, S, 

SEKIHARA, K, SHIONO, H AND KOHNO, H; HITACHI LTD, TOKYO, JAPAN. 

31 DELAYED REFOCUSSING TWO-DIMENSIONAL NMR IN ROTATING SOLIDS; 

*KOLBERT, A C, RALEIGH, D P, LEVITT, M H AND GRIFFIN, R G; MIT, 

CAMBRIDGE, MA. 

32 MEASUREMENTS OF TWO-DIMENSIONAL NMR POWDER PATTERNS IN 

ROTATING SOLIDS; NAKAI, T, ASHIDA, J AND *TERAO, T; KYOTO UNIV, 

KYOTO, JAPAN. 

75

33 INTERPRETATION OF THE NMR NUTATION SPECTRA; *SAMOSON, 

A AND LIPPMAA, E; ESTONIAN ACADEMY OF SCIENCES, TALLINN, USSR. 

34 RF PUMPING EFFECTS IN HEXAMETHYLENETETRAMINE; *SANDERS, J 

P, FINEMAN, M A AND BURNETT, L J; SAN DIEGO STATE UNIV, SAN 

DIEGO, CA. 

35 DYNAMIC NUCLEAR POLARIZATION STUDIES OF A MOLECULARLY DOPED 

POLYMER; WIND, R A, LI, L, MACIEL, G E, *ZUMBULYADIS, N AND 

YOUNG, R H; EASTMAN KODAK CO, ROCHESTER, NY. 

36 FREQUENCY SWITCHED INVERSION PULSES AND THEIR 

APPLICATION TO BROADBAND DECOUPLING; FUJIWARA, T AND *NAGAYAMA, 

K; JEOL LTD, TOKYO, JAPAN. 

37 MOLECULAR MOTIONS IN SOLIDS MEASURED FROM 13C LINEWIDTHS; 

NICELY, V A AND *HENRICHS, P M; EASTMAN KODAK CO, ROCHESTER, NY. 

38 HIGH RESOLUTION ELECTROPHORETIC NMR (ENMR) OF A MIXTURE; 

*SAARINEN, T R AND JOHNSON, C S; UNIV OF NORTH CAROLINA, CHAPEL 

HILL, NC. 

39 2D NMR STUDIES AT 600 MHZ OF A PROTEIN-DNA COMPLEX USING 

IMPROVED TECHNIQUES FOR WATER SUPPRESSION AND HETERONUCLEAR 

CORRELATION SPECTROSCOPY; *OTTING, G, LEUPIN, W, EUGSTER, A AND 

WUTHRICH, K; INST F MOLEKULARBIOLOGIE UND BIOPHYSIK, ZURICH, 

SWITZERLAND. 

40 ALTERNATE METHODS FOR COLLECTION OF 2D-NMR SPECTRA; 

*RINALDI, P AND IVERSON, D; UNIVERSITY OF AKRON, AKRON, OH. 

76

~k 41 A HYPO-RELAXATION AGENT; SIMULTANEOUS USE WITH HYPER- 

RELAXATION AGENTS TO IMPROVE LOCALIZED CONTRAST IN NMR IMAGING; 

*LEE, J P; NEW ENGLAND DEACONESS HOSP, BOSTON, MA. 

42 SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS FOR COBROTOXIN; 

C AND WANG, C; NATIONAL TSING HUA UNIV, HSINCHU, TAIWAN. *YU, 

43 COHERENT AVERAGING THEORY UNDER THE CONDITION OF STRONG 

PULSES OF FINITE WIDTH AND ITS APPLICATION; *XIAOLING, W, 

SHANMIN, Z AND XUEWEN, W; EAST CHINA NORMAL UNIVERSITY, 

SHANGHAI, P R CHINA. 

44 TWO DIMENSIONAL LINEAR PREDICTION NMR SPECTROSCOPY; 

*GESMAR, H AND LED, J J; UNIVERSITY OF COPENHAGEN, COPENHAGEN, 

DENMARK. 

45 INTERGLYCOSIDIC 13C-1H COUPLING CONSTANTS AN APPROACH TO 

DISACCHARIDE AND POLYSACCHARIDE CONFORMATIONS; *MORAT, C AND 

TARAVEL, R F; CARLETON UNIVERSITY, OTTAWA, CANADA. 

46 CARBON-13 SPECTRAL ASSIGNMENTS OF DNA OLIGOMERS APPLICATION 

OF PROTON-DETECTED HETERONUCLEAR 2D-NMR; *ASHCROFT, J AND 

COWBURN, D; THE ROCKEFELLER UNIVERSITY, NEW YORK, NY. 

47 A NEW MODEL FOR HARTMANN-HAHN CROSS RELAXATION IN NMR; *WU, 

X L, *ZHANG, S M AND *WU, X W; EAST CHINA NORMAL UNIV, SHANGHAI, 

P R CHINA. 

48 SEMUT SPECTRAL EDITING, CALIBRATION OF RF FIELD STRENGTHS, 

AND TOSS AT HIGH SPINNING SPEEDS IN 13 C CP/MAS NMR OF SOLIDS; 

*NIELSEN, N C , BILDSOE, H, JAKOBSEN, H J AND SORENSEN, 0 W; 

UNIVERSITY OF AARHUS, ARHUS C, DENMARK. 

7"7

49 CHEMICAL SHIFT IMAGING OF HUMAN INTERNAL ORGANS AT 1.5T; 

*THOMA, W J, TAYLOR, J S, NELSON, S J AND BROWN, T R; FOX CHASE 

CANCER CENTER, PHILADELPHIA, PA. 

50 PIQABLE AUTOMATIC AND RELIABLE QUANTIFICATION OF LOW 

SIGNAL TO NOISE SPECTRA; *NELSON, S J AND *BROWN, T R; FOX 

CHASE CANCER CENTER, PHILADELPHIA, PA. 

51 SOLID STATE NMR INVESTIGATIONS OF CERAMICS AND GLASSES WITH 

EXTREMELY LONG SPIN-LATTICE RELAXATION TIMES; *HAMMOND, T E , 

BOYER, R D AND MOONEY, J R; BP AMERICA RESEARCH & DEVELOPMENT, 

CLEVELAND, OH. 

52 INTERCONVERSION OF VALENCE TAUTOMERS IN CYCLOBUTADIENE- 

13C2 IN AN ARGON MATRIX; *ORENDT, A M, *ARNOLD, B R, 

*RADZISZEWSKI, J G, *FACELLI, J C, *MALSCH, K D, *STRUB, H, 

*GRANT, D M AND *MICHL, J; UNIVERSITY OF UTAH, SALT LAKE CITY, 

UT. 

53 NMR CHEMICAL SHIFT ASSIGNMENTS BY ISOLATION OF MOLECULAR 

CONFORMATIONS IN SOLUTION AT LOW TEMPERATURES PLATINUM- 

PHOSPHINE COMPLEXES; *LUCK, L A, BUSHWELLER, C H AND RHEINGOLD, 

A L; UNIVERSITY OF VERMONT, BURLINGTON, VT. 

54 A 13C CP/MAS AND 2H WIDELINE VARIABLE TEMPERATURE STUDY OF 

BECLOMETHASONE DIPROPIONATE--HEXANE INCLUSION COMPLEX; *EARLY, 

T A AND PUAR, M S; GE NMR INSTRUMENTS, FREMONT, CA. 

55 HUMAN IN VIVO SPECTROSCOPY AT 4.0T; HENTSCHEL, D, 

VETTER, J, LADEBECK, R AND *ALBRIGHT, M J; SIEMENS MEDICAL 

SYSTEMS INC, ISELIN, NJ. 

56 THE SOURCE OF AN ARTIFACT IN THE 1H - 1H DECOUPLED 

HETERONUCLEAR CHEMICAL SHIFT CORRELATION EXPERIMENT; *BAIN, A D, 

HUGHES, D W AND HUNTER, H N; MCMASTER UNIVERSITY, HAMILTON, 

ONTARIO, CANADA. 

78

57 STRUCTURAL STUDIES OF LIPIDS IN FIELD ORDERED MODEL 

MEMBRANES; *RAM, P, *O'BRIEN, P AND PRESTEGARD, J H; YALE 

UNIVERSITY, NEW HAVEN, CT. 

58 MEASUREMENT OF T1 RELAXATION RATES OF COUPLED SPINS VIA 2D 

ACCORDION SPECTROSCOPY WITH APPLICATION TO ACYL CARRIER PROTEIN; 

*KAY, L E, *FREDERICK, A F AND PRESTEGARD, J Hi YALE UNIVERSITY, 

NEW HAVEN, CT. 

59 UNTRUNCATION OF DIPOLE-DIPOLE COUPLINGS IN SOLIDS, OR 

ZERO FIELD NMR ENTIRELY IN HIGH FIELD; *TYCKO, R~ AT&T BELL 

LABORATORIES, MURRAY HILL, NJ. 

60 GLUCOSE METABOLISM IN PERFUSED HEARTS MONITORED BY 13C NMR 

SPECTROSCOPY A MORE SENSITIVE INDICATOR OF ALTERED FLOW THAN 

HIGH ENERGY PHOSPHATE LEVELS~ *CHACKO, V P, WEISS, R G, 

GLICKSON, J D AND GERSTENBLITH, G; JOHN HOPKINS MEDICAL 

INSTITUTIONS, BALTIMORE, MD. 

61 CU NQR OF YBA2CU30X WITH VARYING OXYGEN CONTENT; *VEGA, 

A J, FARNETH, W E, BORDIA, R K AND McCARRON, E M; E I DU PONT 

DE NEMOURS AND COMPANY, WILMINGTON, DE. 

62 MEASUREMENT OF 13C-15N DIPOLAR COUPLINGS IN SOLIDS; *BORK, 

V, GULLION, T, HING, A AND SCHAEFER, J; WASHINGTON UNIVERSITY, 

ST LOUIS, MO. 

63 EFFECT OF 15N PULSE SPACINGS ON 13C-15N REDOR; *GULLION, T 

AND SCHAEFER, J; WASHINGTON UNIVERSITY, ST LOUIS, MO. 

64 MICROSCOPIC IMAGING OF LIVE MOUSE AT 400 MHZ; *SARKAR, S K, 

GREIG, R AND MATTINGLY, M; SMITH KLINE & FRENCH LABORATORIES 

KING OF PRUSSIA, PA. 

79

65 APPLICATION OF A ONE DIMENSIONAL IMAGING EXPERIMENT; 

*BORAH, B AND *SZEVERENYI, N M; NORWICH EATON PHARMACEUTICALS 

INC, NORWICH, NY. 

66 NMR IMAGING TECHNIQUES IN MATERIALS SCIENCE; *CHU, S AND 

FOXALL, D; SPECTROSCOPY IMAGING SYSTEMS, FREMONT, CA. 

67 DEVELOPMENTS IN NITROGEN-14 NMR SPECTROSCOPY; *MCNAMARA, R, 

*RAMANATHAN, K V AND *OPELLA, S J; UNIVERSITY OF PENNSYLVANIA, 

PHILADELPHIA, PA. 

68 CONFORMATIONAL ANALYSIS VIA VICINAL CARBON-HYDROGEN 

COUPLING~ *WATERHOUSE, A; TULANE UNIVERSITY, NEW ORLEANS, LA. 

69 VECTOR GRAPHICS TO DEPICT MULTIPULSE NMR; *WATERHOUSE, A L 

AND *GARBETT, S P; TULANE UNIVERSITY, NEW ORLEANS, LA. 

70 2H NMR STUDIES OF MOTIONS IN SOLIDS D2S AND D2SE; COLLINS, 

M J, *RATCLIFFE, C I AND RIPMEESTER, J A; NATIONAL RESEARCH 

COUNCIL OF CANADA, OTTAWA, ONTARIO, CANADA. 

71 STUDIES OF FLAVODOXIN BY HOMONUCLEAR AND HETERONUCLEAR 

NMR TECHNIQUES; *THANABAL, V AND WAGNER, G; UNIVERSITY OF 

MICHIGAN, ANN ARBOR, MI. 

72 SCUBA, A WAY TOWARDS COMPLETE 1H SPECTRA IN PROTEINS, AND 

EFFICIENT USE OF 15N LABELS IN PROTEINS; *MUELLER, L, WEBER, P 

L AND BROWN, S C; SMITH KLINE & FRENCH LABORATORIES, KING OF 

PRUSSIA, PA. 

80 

2D

73 THE AUTOMATED NMR LABORATORY; SPANTON, S G, FRUEHAN, P AND 

*STEPHENS, R L; ABBOTT LABORATORIES, NORTH CHICAGO, IL. 

74 PH EFFECTS ON THE SOLUTION CONFORMATION OF SHIKIMATE-3- 

PHOSPHATE DETERMINATION BY NMR AND DISTANCE GEOMETRY 

CALCULATIONS; *CASTELLINO, S, LEO, G C AND SAMMONS, R D; 

MONSANTO AGRICULTURAL COMPANY, ST LOUIS, MO. 

75 ASSIGNMENTS OF 31P AND 1H RESONANCES IN OLIGONUCLEOTIDES BY 

TWO DIMENSIONAL HETERONUCLEAR HARTMANN-HAHN SPECTROSCOPY; 

*ZAGORSKI, M G, KALNIK, M W, GAO, X, NORMAN, D AND KOUCHAKDJIAN, 

M; COLUMBIA UNIVERSITY, NEW YORK, NY. 

76 NMR CHARACTERIZATION OF THE GLYPHOSATE-SHIKIMATE-3- 

PHOSPHATE ENZYME DEAD-END COMPLEX; CASTELLINO, S, *LEO, G C, 

SAMMONS, R D AND SIKORSKI, J A; MONSANTO AGRICULTURE COMPANY, 

ST LOUIS, MO. 

77 PULSE SHAPING AND SELECTIVE EXCITATION THE EFFECT OF 

SCALAR COUPLING; *BAZZO, R, BOYD, J AND SOFFE, N; UNIVERSITY 

OF OXFORD, OXFORD, UK. 

78 PHOSPHATE PLASTICIZER DYNAMICS IN GLASSY POLYMER BLENDS BY 

31P CSA LINESHAPES; *INGLEFIELD, P T, JONES, A A, ROY, A K, 

CAULEY, B J AND KAMBOUR, R P; CLARK UNIVERSITY, WORCESTER, MA. 

79 NON UNIFORM SAMPLING IN NMR EXPERIMENTS; MANASSEN, Y AND 

*NAVON, G; TEL AVIV UNIVERSITY, TEL AVIV, ISRAEL. 

80 HIGH RESOLUTION MR IMAGING AT 4.7T OF THE CENTRAL NERVOUS 

SYSTEM IN RATS; *WANG, P C, *MURAKI, A, ARAJAN, S, *WAMBABE, C, 

*GUIDOTTI, A AND *CARVLIN, M~ GEORGETOWN UNIVERSITY, WASHINGTON, 

DC. 

81

81 SODIUM IMAGING OF OCULAR TUMORS; *KOHLER, S J, KOLODNY, N 

H AND BALASUBRAMANIAM, S; HARVARD MEDICAL SCHOOL, BOSTON, MA. 

82 BROADBAND PULSES FOR EXCITATION AND INVERSION IN I=1 

SYSTEMS; *RALEIGH, D P, OLEJNICZAK, E T AND GRIFFIN, R G; 

CAMBRIDGE, MA. 

MIT, 

83 DEUTERIUM NATURAL ABUNDANCE NMR SPECTROSCOPY MONOTERPENE 

BIOSYNTHESIS, THE LINALOOL-LIMONENE CONNECTION; *LEOPOLD, M F, 

EPSTEIN, W W AND GRANT, D M; UNIVERSITY OF UTAH, SALT LAKE CITY, 

UT. 

84 A PROBE WITH HIGHER DECOUPLING EFFICIENCY AND SENSITIVITY 

FOR SOLID STATE NMR EXPERIMENTS; *JIANG, Y J, WOOLFENDEN, W R, 

SHERWOOD, M H, ALDERMAN, D W, PUGMIRE, R J AND GRANT, D M; 

UNIVERSITY OF UTAH, SALT LAKE CITY, UT. 

85 COMPUTER PATTERN MATCHING IN 2D INADEQUATE SPECTRA; 

*CURTIS, J , MAYNE, C L, ALDERMAN, D W, PUGMIRE, R J AND GRANT, 

D M; UNIVERSITY OF UTAH, SALT LAKE CITY, UT. 

86 THE USE OF J-SPECTRUM TYPE PULSE SEQUENCES IN COUPLED 

RELAXATION STUDIES; *FANG, L, MAYNE, C L AND GRANT, D M; 

UNIVERSITY OF UTAH, SALT LAKE CITY, UT. 

87 2D CHEMICAL SHIFT ANISOTROPY CORRELATION SPECTROSCOPY A 

NEW SAMPLE POSITIONING MECHANISM WHICH SIMPLIFIES MEASUREMENT OF 

CHEMICAL SHIFT ANISOTROPIES IN COMPLEX SINGLE CRYSTALS; 

*SHERWOOD, M H, ALDERMAN, D W AND GRANT, D M; UNIVERSITY OF 

UTAH, SALT LAKE CITY, UT. 

88 SOLID STATE 113CD NUCLEAR MAGNETIC RESONANCE STUDY OF 

EXCHANGED MONTMORILLONITES; *BANK, S, BANK, J F AND ELLIS, P D; 

SUNY AT ALBANY, ALBANY, NY. 

82

89 13C NMR ASSIGNMENTS OF DNA OLIGONUCLEOTIDES AND THE DRUG 

NETROPSIN; *BOUDREAU, E, *HYMAN, T, *LAPLANTE, S *MARTIN, G, 

*JACKSON, G AND *BORER, P; SYRACUSE UNIVERSITY, SYRACUSE, NY. 

90 THREE-DIMENSIONAL STRUCTURE DETERMINATION OF DNA 

~D(TAGCGCTA)]2; *WANG, S, DELSUC, M, LEVY, G, BORER, P AND 

LAPLANTE, S; SYRACUSE UNIVERSITY, SYRACUSE, NY. 

91 OPTIMIZATION OF NMR DATAPROCESSING WITH PARALLEL COMPUTERS; 

*HOFFMAN, R E AND LEVY, G C; SYRACUSE UNIVERSITY, SYRACUSE, NY. 

92 CHARACTERIZATION OF NORMAL BRAIN TISSUE USING MRI 

PARAMETERS AND A STATISTICAL ANALYSIS SYSTEM; *HYMAN, T J, 

LEVY, G C, KURLAND, R J AND SHOOP, J D; SYRACUSE UNIVERSITY 

SYRACUSE, NY. 

93 TOWARD A COMPUTER ASSISTED ANALYSIS OF NOESY SPECTRA A 

MULTIVARIATE PATTERN RECOGNITION ANALYSIS OF DNA AND RNA NOESY 

SPECTRA; GRAHN, H, DELAGLIO, F, EDLUND, U, ROGGENBUCK, M W AND 

*BORER, P; SYRACUSE UNIVERSITY, SYRACUSE, NY. 

94 MULTIVARIATE TECHNIQUES FOR ENHANCEMENT OF TWO 

DIMENSIONAL NMR SPECTRA; GRAHN, H, *DELAGLIO, F, ROGGENBUCK, M 

W AND LEVY, G C; SYRACUSE UNIVERSITY, SYRACUSE, NY. 

95 NIH RESOURCE FOR MULTI-NUCLEI NMR AND DATA PROCESSING AT 

SYRACUSE UNIVERSITY; *HEFFRON, G J, LIPTON, A S, BISHOP, K D, 

LAPLANTE, S R, BORER, P N AND LEVY, G C; SYRACUSE UNIVERSITY, 

SYRACUSE, NY. 

96 AN EVALUATION OF NEW PROCESSING PROTOCOLS FOR IN VIVO NMR; 

*MAZZEO, A R AND LEVY, G C; SYRACUSE UNIVERSITY, SYRACUSE, NY. 

83

97 2DNMR DETERMINATION OF 13C SPIN-LATTICE RELAXATION TIMES IN 

BPTI BY INDIRECT DETECTION; *NIRMALA, N R AND WAGNER, G; 

UNIVERSITY OF MICHIGAN, ANN ARBOR, MI. 

98 CHEMICAL EXCHANGE OF HETERONUCLEAR LONGITUDINAL TWO-SPIN 

ORDER (IZSZ) A DYNAMIC PROBE OF CONFORMATIONAL ISOMERIZATION IN 

PROTEINS; *MONTELIONE, G T AND WAGNER, G~ UNIVERSITY OF 

MICHIGAN, ANN ARBOR, MI. 

99 TEACHING MRI USING COMPUTER ANIMATION; *HORNAK, J P; 

ROCHESTER INSTITUTE OF TECHNOLOGY, ROCHESTER, NY. 

100 NOVEL RESONATOR DESIGNS; 

*BRYANT, R G AND *HORNAK, J P; 

TECHNOLOGY, ROCHESTER, NY. 

*MARSHALL, E, *LISTINSKY, J J, 

ROCHESTER INSTITUTE OF 

101 THE USE OF VARIABLE ANGLE SAMPLE SPINNING TO ASSESS 

AROMATIC CLUSTER SIZE IN COALS, COAL CHARS AND CARBONACEOUS 

MATERIALS; *SOLUM, M S, SETHI, N K, FACELLI, J C, WOOLFENDEN, W 

R, PUGMIRE, R J AND GRANT, D M; UNIVERSITY OF UTAH, SALT LAKE 

CITY, UT. 

102 STRONG 181TA QUADRUPOLE INTERACTIONS DETECTED VIA CROSS- 

RELAXATION TO HYDROGEN BY PROTON SPIN-LATTICE RELAXATION RATE 

STUDY IN TAH.322; *TORGESON, D R, HAN, J-W AND BARNES, R G; 

IOWA STATE UNIVERSITY, AMES, IA. 

103 PRE-PULSE SEQUENCE - AN INVERSION PULSE T (Y) AND A DELAY 

TIME ( T3); *LIN, F T AND LIN, F M; UNIVERSI OF PITTSBURGH, 

PITTSBURGH, PA. 

104 TAYLOR TRANSFORMATION OF 2D NMR M SERIES FROM TIME 

DIMENSION TO POLYNOMIAL DIMENSION FOR CONVENIENT DETERMINATION 

OF CROSS RELAXATION RATES IN NOESY SPECTRA; *HYBERTS, S G AND 

WAGNER, G; UNIVERSITY OF MICHIGAN, ANN ARBOR, MI. 

84

105 EVALUATION OF DOUBLE TUNED CIRCUITS USED IN NMR; 

VARIAN ASSOCIATES, PALO ALTO, CA. 

*ZENS, T; 

106 ARTIFACTS IN ECHO-PLANAR IMAGING; *AVRAM, H E, CROOKS, L 

E AND KRAMER, D M; DIASONICS MRI, SOUTH SAN FRANCISCO, CA. 

107 TWO DIMENSIONAL NMR SOFTWARE IN THE WORKSTATION 

ENVIRONMENT; *DELAGLIO, F, SOLE, P, GRAHN, H, MACUR, A, 

BEGEMANN, J, CROWTHER, M, HOFFMAN, R AND LEVY, G C; NEW METHODS 

RESEARCH INC, SYRACUSE, NY. 

108 PERFORMANCE COMPARISON OF DOUBLE-TUNED SURFACE COILS; 

*FITZSIMMONS, J R, BROOKER, H R, KUAN, W AND BECK, B; UNIV OF 

FLORIDA, GAINESVILLE, FL. 

109 NMR STUDY OF ALKALINE HYDROLYSIS OF POLY-(ACRYLONITRILE) 

*LOVY, J AND STOY, V; KINGSTON TECHNOLOGIES INC, DAYTON, 

110 DISCRETE ANALYSIS OF STOCHASTIC NMR USING WIENER SERIES; 

*WONG, S T S, NEWMARK, R D AND ROOS, M S; UNIV OF CALIFORNIA, 

BERKELEY, CA. 

111 STOCHASTIC NMR IMAGING WITH OSCILLATING GRADIENTS; 

S T S, *ROOS, M S AND NEWMARK, R D; UNIV OF CALIFORNIA, 

BERKELEY, CA. 

WONG, 

112 RECENT EXTENSIONS OF NOESYSIM, A PROGRAM FOR RAPID 

COMPUTATION OF NOESY INTENSITY MATRICES FROM ATOMIC COORDINATES 

AND EXPERIMENTAL CONDITIONS; *EATON, H L, ANDERSEN, N H AND LAI, 

X; UNIV OF WASHINGTON, SEATTLE, WA. 

B5

113 31P MAGENTIC RESONANCE IMAGING OF SOLID CALCIUM PHOSPHATES: 

POTENTIAL FOR CHEMICAL IMAGING OF BONE; ACKERMAN, J L, *RALEIGH, 

D P AND GLIMCHER, M J; MIT, CAMBRIDGE, MA. 

114 VOLUME LOCALIZED SPECTRAL EDITING USING ZERO QUANTUM 

COHERENCE CREATED IN A STIMULATED ECHO PULSE SEQUENCE; *SOTAK, 

C H AND FREEMAN, D M; GE NMR INSTRUMENTS, FREMONT, CA. 

115 USE OF PURE ABSORPTION PHASE 31P/1H 2D COLOC NMR SPECTRA 

FOR ASSIGNMENT OF 31P SIGNALS OF OLIGONUCLEOTIDES; FU, J M, 

SCHROEDER, S A, JONES, C R, SANTINI, R AND *GORENSTEIN, D G; 

PURDUE UNIV, W LAFAYETTE, IN. 

116 MODIFICATION TO A JEOL GX270 WIDEBORE SPECTROMETER FOR 

MAGNETIC RESONANCE IMAGING: PETROGRAPHIC APPLICATIONS; *DOUGHTY, 

D A AND MAEREFAT, N L; NIPER, BARTLESVILLE, OK. 

117 RESONANT EFFECTS IN CP-MAS SPECTRA OF HOMONUCLEAR DIPOLAR- 

COUPLED SPIN SYSTEMS; *BARBARA, T M AND HARBISON, G S; SUNY, 

STONY BROOK, NY. 

118 APPLICATION OF N-H HETERONUCLEAR CORRELATION SPECTROSCOPY 

TO SEVERAL 15N ENRICHED PROTEINS; *MOOBERRY, E S, STOCKMAN, B J, 

YUAN, B, OH, B H AND MARKLEY, J L; UNIV OF WISCONSIN, MADISON, 

WI. 

119 13C LABELING AND HIGH RESOLUTION 1H 2-D NMR: MAKING 

UNNATURAL ESTERS STAND UP AND BE COUNTED; *HELMS, G L, 

NIEMCZURA, W P AND MOORE, R E; UNIV OF HAWAII, HONOLULU, HI. 

120 SPECIATION OF WATER IN GLASSES BY HIGH-SPEED 1H MAS-NMR; 

*ECKERT, H, YESINOWSKI, J P, SILVER, L A AND STOLPER, E M; UNIV 

OF CALIFORNIA, SANTA BARBARA, CA. 

8B

121 BROADBAND SPIN DECOUPLING IN THE PRESENCE OF SCALAR 

INTERACTIONS; *SHAKA, A J, LEE, C J AND PINES, A; UNIV OF 

CALIFORNIA, BERKELEY, CA. 

122 MULTINUCLEAR TWO-DIMENSIONAL APPROACHES TO SEQUENCE- 

SPECIFIC RESONANCE ASSIGNMENTS IN A PROTEIN" 13C-13C, 13C-15N, 

1H-13C, 1H-15N, AND 1H-1H CORRELATIONS IN ANABAENA 7120 

FLAVODOXIN; *STOCKMAN, B J, WESTLER, W M, MOOBERRY, E S AND 

MARKLEY, J L; UNIV OF WISCONSIN, MADISON, WI. 

123 SOLID STATE NUCLEAR MAGNETIC RESONANCE INVESTIGATIONS OF 

ORGANOPHOSPHONIC ACID ADSORPTION ON ALUMINA; *DANDO, N R, 

WEISERMAN, L F AND MARTIN, E S; ALCOA TECH CENTER, ALCOA CENTER, 

PA. 

124 A COMPLETELY INTEGRATED NETWORK OF HOME-BUILT AND 

COMMERCIAL NMR SPECTROMETERS~ *BOUCHARD, D A AND OPELLA, S J; 

UNIV OF PENNSYLVANIA, PHILADELPHIA, PA. 

125 NMR VS CIRCULAR DICHROISM: WHAT CAN WE SAY ABOUT HELICITY?; 

*BEHLING, R W, MIRAU, P A AND JELINSKI, L W; AT&T BELL LABS, 

MURRAY HILL, NJ. 

126 EXPERIMENTAL EVALUATION OF NMR IMAGING PROBES; *TALAGALA, 

S L AND HALL, L D; UNIV OF BRITISH COLUMBIA, VANCOUVER, CANADA. 

127 HETERONUCLEAR TWO-DIMENSIONAL NMR METHODS FOR THE 

DETERMINATION OF THE PRIMARY STRUCTURE OF PEPTIDES; BORNEMANN, 

V, CHESNICK, A S, HELMS, G, MOORE, R E AND *NIEMCZURA, W P; 

UNIV OF HAWAII, HONOLULU, HI. 

128 VOLUME-SELECTIVE SIGNAL SUPRESSION IN SURFACE-COIL NMR 

SPECTROSCOPY" COMPARISON OF THREE MEHTODS; SMITH, C D, THOMAS, 

G S AND *SMITH, S L; UNIV OF KENTUCKY, LEXINGTON, KY. 

87

129 IN VIVO VOLUME LOCALIZED SURFACE COIL SPECTROSCOPY WITH 

ISIS AND DRESS: THE CHEMICAL SHIFT DISPLACEMENT; SMITH, C D, 

THOMAS, G S AND *SMITH, S L; UNIV OF KENTUCKY, LEXINGTON, KY. 

130 SEQUENTIAL ASSIGNMENT OF AMIDE PROTONS IN -HELICES IN 

LARGE PROTEINS; *SPARKS, S W, BAX, A AND TORCHIA, D A~ NIH, 

BETHESDA, MD. 

131 MASS TRANSFER PROCESSES STUDIED BY NMR IMAGING; HALL, L D 

AND *WEBB, A G; ADDENBROOKES HOSP, CAMBRIDGE, ENGLAND. 

132 NATURAL ABUNDANCE 13C AND 14N NMR OF BACTERIAL 

OSMOLYTES IN VIVO; *LEWIS, B A, CAYLEY, S C, PADMANABHAN, S AND 

RECORD, M T; UNIV OF WISCONSIN, MADISON, WI. 

133 CHARACTERIZATION OF HUMAN BLOOD PLASMA USING VERY HIGH 

FIELD RESOLUTION ENHANCED PRM DIFFERENCE SPECTROSCOPY; *DADOK, 

~ BOTHNER-BY, A A, MISHRA, P, WILKINSON, D A, GILES, R H, 

EVEDO, H F, SHRIVASTAVA, P N AND JARAMILLO, B; CARNEGIE 

MELLON UNIV, PITTSBURGH, PA. 

134 PERFUSION PROBE FOR A BRUKER AM-400 WIDE-BORE SPECTROMETER; 

*ANDERSON, M E, CHOBANIAN, M, MOOBERRY, E S, MARKLEY, J L AND 

ARUS, C; UNIV OF WISCONSIN, MADISON, WI. 

135 HOMONUCLEAR TWO DIMENSIOANL 13C DOUBLE QUANTUM CORRELATION 

SPECTROSCOPY (2D 13C{13C}DQC AND IH-{13C}HETCOR AS PRIMARY TOOLS 

FOR SPIN SYSTEM AND HEME ASSIGNMENTS IN CYTOCHROME C553; *REILY, 

M D, ULRICH, E L, WESTLER, W M AND MARKLEY, J L" UNIV OF 

WISCONSIN, MADISON, WI. 

136 THREE-DIMENSIONAL STRUCTURE OF TURKEY OVOMUCOID THIRD 

DOMAIN BY 2D-NMR SPECTROSCOPY AND DISTANCE GEOMETRY CALCULATIONS; 

*DARBA, P, KREZEL, A FEJZO J, MACURA S, ROBERTSON, A D AND 

MARKLEY, J L; UNIV 6F WISC6NSIN, MADISON, WI. 

88

137 TWO-DIMENSIONAL 13C{15N}, 13C{13C} AND 1H{13C} CHEMICAL 

SHIFT CORRELATION IN PROTEINS: SEQUENCE-SPECIFIC ASSIGNMENT OF 

RESONANCES IN 13C AND 15N-LABELED STREPTOMYCES SUBTILISIN 

INHIBITOR; *WESTLER, W M, KAINOSHO, M, NAGAO, H, TOMONAGA, N 

AND MARKLEY, J L; UNIV OF WISCONSIN, MADISON, WI. 

138 FERREDOXIN FROM ANABAENA 7120" UNIFORM CARBON-13 AND/OR 

NITROGEN-15 ENRICHMENT AND NUCLEAR MAGNETIC RESONANCE 

INVESTIGATIONS; *OH, B H, WESTLER, W M, DARBA, P AND MARKLEY, J 

L; UNIV OF WISCONSIN, MADISON, WI. 

139 TWO-DIMENSIONAL HYDROGEN-I NUCLEAR MAGNETIC RESONANCE 

STUDIES OF STAPHYLOCOCCAL NUCLEASE- SPIN SYSTEM ASSIGNMENTS IN 

THE (NUCLEASE H124L).DEOXYTHYMIDINE-3',5'-BISPHOSPHATE CA2+ 

TERNARY COMPLEX; *WANG, J AND MARKLEY, J L; UNIV OF WISCONSIN, 

MADISON, WI. 

140 DIRECT OBSERVATION OF LONG RANGE HETERONUCLEAR SPLITTINGS 

IN PROTON 2DJ SPECTRA; PRATUM, T K, *HAMMEN, P K AND ANDERSEN, 

N H; UNIV OF WASHINGTON, SEATTLE, WA. 

141 BRANCH LOCATION STUDIED BY SOLVENT SWELLING AND SOLID 

STATE NMR IN ISOTOPICALLY ENRICHED ETHYLENE-I-BUTENE COPOLYMERS; 

*MCFADDIN, D; QUEEN'S UNIV, ONTARIO, CANADA. 

142 INDIRECT DETECTION OF 14N 

*GARROWAY, A N AND MILLER, J B; 

DC. 

M=2 (OVERTONE) NMR TRANSITIONS; 

NAVAL RESEARCH LAB, WASHINGTON, 

143 DIFFERENTIAL DEVELOPMENT OF MULTIPLE-QUANTUM COHERENCE IN 

A L!QUID CRYSTAL; *GERASIMOWICZ, W V, GARROWAY, A N AND MILLER 

J B, NAVAL RESEARCH LAB, WASHINGTON, DC. 

144 1H AND 13C REFOCUSED GRADIENT IMAGING OF SOLIDS; *MILLER, 

J B AND GARROWAY, A N; NAVAL RESEARCH LAB, WASHINGTON, DC. 

89

145 DERIVATION OF POLYMER RHEOLOGICAL CONSTANTS FROM THE 

VISCOSITY AND TEMPERATURE DEPENDENCE OF 13C NMR RELAXATION 

PARAMETERS; *BRANDOLINI, A J; MOBIL CHEMICAL CO, EDISON, NJ. 

146 SOME APPLICATIONS OF THE WATR EXPERIMENT; *RABENSTEIN, D 

L, GUO, W AND SMITH, E; UNIV OF CALIFORNIA, RIVERSIDE, CA. 

147 THERMALLY INDUCED VOLUME CHANGES IN A BLOCK COPOLYMER; 

*CAU, F AND LACELLE, S; UNIV DE SHERBROOKE, QUEBEC, CANADA. 

148 CHALLENGES TO THE CLASSICAL MODELS OF REACTIVITY; 

B; CORNELL UNIV, ITHACA, NY. 

149 19F NMR STUDIES OF FLUORINE SUBSTITUTED Ba2YCu307-x; 

C E, WHITE, D, DAVIES, P K AND STUART, J A; UNIV OF 

PENNSYLVANIA, PHILADELPHIA, PA. 

*LYONS, 

150 ISOTOPE DETECTED NOE EXPERIMENTS ON 13C LABELED tRNA Phe; 

*GMEINER, W H AND POULTER, C D; UNIV OF UTAH, SALT LAKE CITY, 

UT. 

151 INVERSION RECOVERY CROSS POLARIZATION NMR STUDY OF 

MORPHOLOGY IN POLYETHYLENES; *YANG, T S AND RITCHEY, W M; 

WESTERN RESERVE UNIV, CLEVELAND, OH. 

*LEE, 

CASE 

152 NMR STUDY OF NAPHTHALENE TRANSPORT AND RELAXATION IN THE 

NAPHTHALENE-SUPERCRITICAL ETHYLENE SYSTEM~ *WOO, K W, ADAMY, S 

AND JONAS, J; UNIV OF ILLINOIS, URBANA, IL. 

90

153 NMR CHARACTERIZATION OF THE SOLUTION, GEL AND SOLID 

STRUCTURES OF [(1-3)-B-D-GLUCAN (CURDLAN)]; BOLTON, P H, 

*GIAMMATTEO, P J AND STIPANOVIC, A J; TEXACO INC, BEACON, NY. 

154 DISCRIMINATION BETWEEN SYMMETRIC AND ASYMMETRIC HYDROGEN 

BONDS BY ISOTOPIC PERTURBATION OF EQUILIBRIUM; PERRIN, C L AND 

*THOBURN, J D; UCSD, LA JOLLA, CA. 

155 NMR STUDIES OF PHOSPHATIDYLCHOLINES AND 

THIOPHOSPHATIDYLCHOLINES; *BASTI, M M AND LAPLANCHE, L A; 

NORTHERN ILLINOIS UNIV, DEKALB, IL. 

156 ROTATING FRAME COHERENCE TRANSFER DUE TO TUNNELLING; 

*JOHNSTON, E R; HAVERFORD COLLEGE, HAVERFORD, PA. 

157 INTACT STRUCTURE OF ACLACINOMYCIN-A; 

AND CHARI, M; RICE UNIV, HOUSTON, TX. 

*KOOK, A M, ARORA, S 

158 SOME TRICKS OF THE TRADE FOR BETTER 2D NMR SPECTRA (OU 

COMMENT MONTER UNE MAYONNAISE A LA MAIN..); *MARION, D AND BAX, 

A; NIH, BETHESDA, MD. 

159 DEVELOPMENT OF FLUORINATED, NMR ACTIVE SPIN TRAPS FOR 

STUDIES OF FREE RADICAL CHEMISTRY; *SELINSKY, B S, LEVY, L A, 

MOTTEN, A G AND LONDON, R E; NIEHS, RESEARCH TRIANGLE PARK, NC. 

160 A 27AL MAS STUDY OF AMORPHOUS ANODIC ALUMINA: STRUCTURAL 

INFORMATION COMBINED WITH QUANTITATIVE UNCERTAINTY; *FARNAN, I, 

DUPREE~ R, SMITH, M E, JEONG, Y S AND THOMPSON, G; STANFORD 

UNIV, STANFORD, CA. 

91

161 LOCALIZED PROTON SPECTROSCOPY AND SPECTROSCOPIC IMAGING OF 

THE HUMAN BRAIN; *LUYTEN, P AND HOLLANDER, J D; PHILIPS 

MEDICAL SYSTEMS, BEST, THE NETHERLANDS. 

162 HIGH RESOLUTION 13C-1H SHIFT CORRELATION WITH FULL 1H-1H 

DECOUPLING; *PERPICK-DUMONT, M, REYNOLDS, W F AND ENRIQUEZ, R G; 

UNIV OF TORONTO, TORONTO, CANADA. 

163 13C AND 15N MASS SPECTRA OF LABELED STAPHYLOCCOCAL 

NUCLEASE CRYSTALS; *COLE, H B R AND TORCHIA, D A; NIH, 

BETHESDA, MD. 

164 MODIFICATION OF A BRUKER WH-300 SPECTROMETER FOR BROADBAND/ 

HIGH POWER SOLID STATE NMR EXPERIMENTS; *SIMPLACEANU, V AND HO, 

C; CARNEIGE MELLON UNIV, PITTSBURGH, PA. 

165 IN VIVO PHOSPHOROUS-31NMR STUDIES OF HUMAN BRAIN AT 1.5T; 

*KAPLAN, D, PANCHALINGAM, K, MCEVOY, J, SPIKER, D, KESHAVAN, M S, 

WOLF, G E AND PETTEGREW, J; PITTSBURGH NMR INST, PITTSBURGH, PA. 

166 SOLID STATE NMR STUDY ON THE STRUCTURE OF GRAMICIDIN A; 

*TENG Q NORTH, C L, BRENNEMAN, M T, LOGRASSO, P V AND CROSS, T 

A; FLORIDA STATE UNIV, TALLAHASSEE, FL. 

167 DYNAMICS OF THE GRAMICIDIN A TRANSMEMBRANE CHANNEL BY 

SOLID STATE 15N NMR; NICHOLSON, L K, BRENNEMAN, M T, LOGRASSO, 

P V AND *CROSS, T A; FLORIDA STATE UNIV, TALLAHASSEE, FL. 

168 IN VIVO 31P AND 1H NMR SPECTROSOCPY AND IMAGING OF RAT 

LIVER EXPOSED TO HALOCARBONS; TOWNER, R A, *BRAUER, M, FOXALL, 

D AND JANZEN, E G; UNIV OF GUELPH, GUELPH, CANADA. 

92

169 SPECTROSCOPY WITH EXACT APODIZATION TRANSFORMATION (SWEAT); 

*LISICKI, M, BOTHNER-BY, A A, SHUKLA, R, DADOK, J AND VAN ZIJL, 

P C M; CARNEIGE MELLON INST, PITTSBURGH, PA. 

170 FLOW-COMPENSATED NMR IMAGING TECHNIQUES FOR RHEOLOGY OF 

SUSPENSIONS; *MAJORS, P D, ALTOBELLI, S A, FUKUSHIMA, E AND 

GIVLER, R C; LOVELACE MEDICAL FOUNDATION, ALBUQUERQUE, NM. 

171 RAPID ROTATING FRAME IMAGING WITH RETENTION OF CHEMICAL 

SHIFT INFORMATION; MACDONALD, P M, *METZ, K R AND BOEHMER, J P; 

HARVARD MEDICAL SCHOOL, BOSTON, MA. 

172 MAGIC ANGLE SPINNING SEPARATED LOCAL FIELD SPECTROSCOPY: 

SOME EXPERIMENTAL OBSERVATIONS RELEVANT TO THE DETERMINATION OF 

C-H DISTANCES BY NMR; *WEBB, G G AND ZILM, K W; YALE UNIV, HEW 

HAVEN, CT. 

173 DETERMINATION OF H-H BOND DISTANCES IN TRANSITION METAL 

DIHYDROGEN COMPLEXES BY SOLID STATE NMR; CHINN, M, COZINE, M, 

HEINEKEY, M, KUBAS, G, *MILLAR, J AND ZILM, K; YALE UNIV, NEW 

HAVEN, CT. 

174 DESIGN OF A HIGH RESOLUTION HIGH PRESSURE DOUBLE RESONANCE 

NMR PROBE; *GRANDINETTI, P J, VANDERVELDE, D, XIE, C-L, WALKER, 

N A AND JONAS, J; UNIV OF ILLINOIS, URBANA, IL. 

175 CARBON-13 CP/MAS NMR STUDY OF THE NYLON-6 POLYMOPHS AND 

DYNAMICS; *WANG, D, HU, J, YAN, X, WANG, G AND QIAN, B; WUHAN 

INST OF PHYSICS, HUBEI, PR CHINA. 

176 SINGLE CRYSTAL NMR STUDIES OF 113CD COMPLEXES AND 113CD 

NMR OF CADMIUM PROTOPORPHYRIN IX AND CADMIUM MYOGLOBIN; 

*KENNEDY, M A AND ELLIS, P D; UNIV OF SOUTH CAROLINA, COLUMBIA, 

SC. 

93

177 THE ADSORPTION OF Rb+ AND Cs+ TO TRANSITION ALUMINAS BY 

87Rb AND 113Cs SOLID STATE NMR SPECTROSCOPY; *CROCKETT, B AND 

ELLIS, P D; UNIV OF SOUTH CAROLINA, COLUMBIA, SC. 

178 CROSS-POLARIZATION MAS NMR OF 27AI IN - AND -ALUMINA; 

*MORRIS, H D AND ELLIS, P D; UNIV OF SOUTH CAROLINA, COLUMBIA, 

SC. 

179 DYNAMICS OF CHAIN SEGMENTS IN THERMOSET RESINS; *FRY, C G 

AND LIND, A C; MCDONNELL DOUGLAS RES LABS, ST LOUIS, MO. 

180 170/1H NMR MICROSCOPY AT CWRU; *MATEESCU, G, YVARS, G, 

PAZARA, D AND ALLDRIDGE, N A; CASE WESTERN RESERVE, CLEVELAND, 

OH. 

181 APPLICATION OF I-D AND 2-D SODIUM-23 MAGNETIZATION 

TRANSFER NMR TO STUDY TRANSMEMBRANE CATION EXCHANGE; *SHUNGU, D 

C AND BRIGGS, R W; UNIV OF FLORIDA, GAINESVILLE, FL. 

182 SUPPRESSION OF ARTIFACTS IN MULTIPLE ECHO NUCLEAR MAGNETIC 

RESONANCE; *BARKER, G J AND MARECI, T H; UNIV OF FLORIDA, 

GAINESVILLE, FL. 

183 QUANTITATION OF EXCHANGE RATES USING THE RED NOESY 

SEQUENCE; *COCKMAN, M D AND MARECI, T H; UNIV OF FLORIDA, 

GAINESVILLE, FL. 

184 MULTINUCLEAR NMR METHODOLOGY FOR DECONVOLUTING NATURAL 

MIXTURES AND CATALYTICALLY ACTIVE LAYER SILICATES; *THOMPSON, A 

R, CARRADO, K A AND BOTTO, R E; ARGONNE NATL LAB, ARGONNE, IL. 

94

185 PARSING THE EDITED 1H NMR SIGNALS INTO 12C-IH AND 13C-IH 

SUBSPECTRA" A STRATEGY TO STUDY SPECIFIC ACTIVITY IN VIVO; 

*JUE, T; YALE UNIV, NEW HAVEN, CT. 

186 THE 13C RELAXATION BEHAVIOR OF ETHANE THROUGH ITS 

CRITICAL POINT; EVILIA, R F, WHITTENBURG, S L AND *ROBERT, J M; 

LEHIGH UNIV, BETHLEHEM, PA. 

187 NMR INVESTIGATION OF THE CYCLOPHILIN-CYCLOSPORIN COMPLEX~ 

*HEALD, S L, GOOLEY, P R, ARMITAGE, I M, JOHNSON, W C, HARDING, 

M W AND HANDSCHMACHER, R E; YALE UNIV, HEW HAVEN, CT. 

188 INHIBITION OF ALANINE RACEMASE BY THE PHOSPHATE ANALOG OF 

ALANINE, 1-(AMINOETHYL)PHOSPHATE (ALA-P): IDENTIFICATION OF A 

SCHIFF BASE LINKAGE IN THE ENZYME-INHIBITOR COMPLEX BY SOLID 

STATE 15N-NMR; *COPIE, V, FARACI, W S, WALSH, C T AND GRIFFIN, 

R G; MIT, CAMBRIDGE, MA. 

189 DYNAMIC AND CONFROMATIONAL STRUCTURE OF CORD FACTOR 

GLYCOLIPIDS IN MODEL MEMBRANES AS DETERMINED BY SOLID-STATE 2H 

NMR; *BYRD, R A AND LIM, T K; US FDA, BETHESDA, MD. 

190 THE VISUALIZATION OF PROBE ELECTRIC FIELDS; 

AND CHEN, C-N; NIH, BETHESDA, MD. 

*HOULT, D I 

191 NMR ANALYSIS AND IMAGING OF OIL CORES; *EDELSTEIN, W A, 

VINEGAR, H J, ROEMER, P B, TUTUNJIAN, P N AND MUELLER, 0 M; GE 

CORPORATE RES & DEV CENTER, SCHENECTADY, NY. 

192 RESOLUTION ENHANCEMENT OF PHOSPHORUS-31 SPECTRA: THE USE 

OF CDTA IN PERCHLORIC ACID EXTRACTS OF DICTYOSTELIUM DISCOIDEUM; 

*WILLIAMSON, K L AND FROMM, E F; MOUNT HOLYOKE COLLEGE, SOUTH 

HADLEY, MA. 

95

193 ADDITIVITY OF CARBON-13 SPIN-LATTICE RELAXATION TIMES IN 

OCTENES; *WILLIAMSON, K L, SIMONDS, M A AND STENGLE, T R; 

MOUNT HOLYOKE COLLEGE, SOUTH HADLEY, MA. 

194 CPMAS ANALYSIS OF A POLYIMIDE/GLASS CIRCUIT BOARD; *MYERS- 

ACOSTA, B L AND SELOVER, S J; LOCKHEED SPACE CO, SUNNYVALE, CA. 

195 A STUDY ON 3',5'-AMP BY TWO-DIMENSIONAL DOUBLE QUANTUM 

SPECTROSCOPY IN 'H NMR; *WU, G, GUO, W, HUANG, Y, JIANG, S AND 

LIAN, S; YORK UNIV, NORTH YORK, CANADA. 

196 TRIFLUOROETHOXY DERIVATIVES: SELECTIVE DEACTIVATION OF 

OXYGEN CONTAINING FUNCTIONAL GROUPS IN LANTHANIDE INDUCED SHIFTS 

AND/OR RELAXATION NMR STUDIES; *WILD, C, TSIAO, C, GLASS, T E, 

ROY, J AND DORN, H C; VPI&SU, BLACKSBURG, VA. 

197 TIME DOMAIN ENDOR STUDIES OF DISORDERED SOLIDS; 

TINDALL, P J, BERNARDO, M AND *THOMANN, H; EXXON CORP RES LAB, 

ANNANDALE, NJ. 

198 NUMERICAL STUDIES OF STIMULATED ESEEM WAVEFORMS; 

AND *THOMANN, H; EXXON CORP RES LAB, ANNANDALE, NJ. 

JIN, H 

199 HIGH PRESSURE 13C CROSS-POLARIZATION AND SPIN RELAXATION 

STUDY OF ADAMANTANE; *PRINS, K 0 AND VAN DER PUTTEN, D; UNIV 

OF AMSTERDAM, AMSTERDAM, THE NETHERLANDS. 

200 INTERPRETATION OF 13C NMR MIXTURE SPECTRA BY MULTIVARIATE 

ANALYSIS; *BREKKE, T, KVALHEIM, 0 M AND SLETTEN, E; UNIV OF 

BERGEN, BERGEN, NORWAY. 

9B

. z 

201 THE CORRELATION OF 1H-19F COUPLINGS BY HETERONUCLEAR MODE 

PULSED DECOUPLING (HUMPD); *GRODE, S H AND GILLIS, R W; THE 

UPJOHN CO, KALAMAZOO, MI. 

202 SOLID STATE BACK PROJECTION IMAGING; LISTERUD, J AND 

*DROBNY, G; UNIV OF WASHINGTON, SEATTLE, WA. 

203 LONG-RANGE SHIELDING AND CHEMICAL SHIFT IN SILICON CARBIDE 

POLYTYPES; RICHARDSON, M F, *HARTMAN, J S AND GUO, D; BROCK 

UNIV, ONTARIO, CANADA. 

204 RECENT PROGRESS IN HIGH RESOLUTION NMR OF SOLIDS; 

*BRONNIMANN, C E, DEC, S L, FRYE, J S, HAWKINS, B L AND MACIEL, 

G E; COLORADO STATE UNIV, FT. COLLINS, CO. 

205 HIGH-FIELD PULSED GRADIENT DIFFUSION MEASUREMENTS; 

R L AND SCHLEICH, T; UNIV OF CALIFORNIA, SANTA CRUZ, CA. *HANER, 

206 THE WORLD AND WONDERS OF 3H NMR SPECTROSCOPY; 

*WILLIAMS, P G; UNIV OF CALIFORNIA, BERKELEY, CA. 

97

1 I~ I SOLID PHASE CARBON-13 NMR STUDIES OF CROWN ETHERS AND THEIR 

COMPLEXES. G.W. Buchanan*, C. Morat and R.A. Kirby, Ottawa-Carleton Chemistry 

Institute, Dept. of Chemistry, Carleton University, Ottawa Canada KIS 586. 

C.I. Ratcliffe and J.A. Ripmeester, Chemistry Division, N.R.C. Ottawa Canada KIA ORg. 

For a series of 12-crown-4, 14-crown-4 and 18-crown-6 ethers, i~C CPMAS spectra 

have been used to determine the asymmetric units present in the crystals. Results 

are compared wfth those available from x-ray crystallographic data. In several 

18-crown-6 complexes, low temoerature spectra have been recorded which reflect 

retardation, on the NMR timescale, of rotational motion oresent in the solids at 

298K. Torsional angle contributions to the observed 13C chemical shifts at low 

temperature will be delineated. 

I 

-- 2 I A NEW APPROACH FOR QUANTITATIVE 13C-NMR SPECTROSCOPY OF COALt: 

Robert E. Botto*, John V. Muntean and Leon M. Stock, Chemistry Division, Argonne 

National Laboratory, 9700 South Cass Avenue, Argonne, Illinois 60439. 

Several researchers recently have discussed the scope and limitations of solid 

13C-NMR spectroscopy for the analysis of fossil fuels. Several, including our- 

selves, have established that only 50-70% of the 13C nuclei in coals are observed 

in Bloch-decay or CP/MAS solid NMR experiments. This poster concerns recent work 

from our laboratories directed toward the achievement of more quantitative 

spectroscopic results. One phase of our work centers on the use of tetrakis(tri- 

methylsilyl)silane as a qualitative chemical shift standard and as a quantitative 

internal standard for the measurement of the observable quantity of 13C nuclei. 

The other phase of this study focuses on the application of samarium(ll) iodide 

for the selective removal of organic free radicals from coal. Reduction of the 

radical content is essential for the realization of quantitative spectroscopic 

results. 

tWork performed under the auspices of the Office 

Sciences, Division of Chemical Sciences, U.S. Department 

contract number W-31-I09- ENG-38. 

98 

of Basic Energy 

of Energy, under

i m 3 I 

31p SOLID STATE NMR STUDIES OF ZrP, Mg3P2, MgP4, AND CdPS3, 

R. A. Nissan* and'T. A. Vanderah, Chemistry Division, Research Department, 

Naval Weapons Center, China Lake, CA 93555. 

The 31p solid state NMR spectra of ZrP, Mg3P2, MgP4, and CdPS3 are reported. Static and marc 

angle spinning (MAS) spectra were obtained for each compound. In all cases, chemical shift anisotropy and 

the effects of dipolar broadening were sufficiently reduced by the MAS method to reveal the isotropic 

hemical shifts for each crystallographically distinct phosphorus. The observed resonances were assigned to 

he different types of phosphorus by considering the structural details of each compound. In ZrP the two 

.'hemical shifts of +128.4 and +187.5 ppm (relative to 85% H3PO4) were assigned to P occupying the 

¢¢yckoff 2d and 2a sites, respectively. Assignments were confirmed by quenching of ZrP0.92 thus 

mriching the 2a site. In Mg3P2, two resonances from the 24d and 8a site P atoms were observed at -262.3 

md -239.6 ppm, respectively. In MgP4 two types of phosphorus, one type coordinated to two Mg and two 

P and the other to three P and one Mg, gave chemical shifts of-109.2 and -6.1 ppm, respectively. From 

,?.dPS3 only one resonance at +104.9 ppm is observed as all P atoms are crystallographically:equivalent. 

I HIGH RESOLUTION SPECTRA OF LIQUIDS IN INHOMOGENEOUS ENVIRONMENTS 

AS OBTAINED BY MASS 

V. Rutar, Department of Chemistry, Iowa State University, Ames, Iowa 50011 

Magic angle sample spinning successfully reduces line broadening arising from 

differences in magnetic susceptibility. Although this advantage seems 

superficial in NMR spectroscopy of solids, it offers interesting new 

possibilities in studies of some "liquid-like" samples. Many biological systems 

represnet significant examples where MASS improves resolution and sensitivity. 

IH and 13C spectra of plant seeds facilitate nondestructive determination of oil 

composition thus allowing rapid development of better varieties. Detection of 

dissolved sugars monitors germination processes without destroying the sample. 

MASS of liquids can be applied also to other objects which are small enough to 

fit into the spinner cavity (typical volume is about 1 cm~), because spinning 

frequencies are moderate (100-500 Hz). Precise balancing of rotors is not 

essential and mechanical stress does not appear dangerous. 

99

S 

Pascale Sole*, a b 

Frank Delaglio, a' 

George C. Levy, b 

I 

CONSTRAINED DECONVOLUTION OF 2D NMR SPECTRA AND IMAGES 

a 

b New Methods Research, Inc., 719 E. Genesee Street, Syracuse, NY 13210 

Syracuse University, Department of Chemistry, Syracuse, NY 13210 

We have been examining a fast constrained deconvolution method used to 

achieve better resolution in 2D spectra and images. The method uses 

estimates of the noise mean and variance in conjunction with a 

criterion of spectral quality to reconstruct the 'best' result. The 

quality criterion is a smoothness constraint, such as the minimization 

of the second derivative amplitude or a maximization of the entropy of 

the spectrum. Both approaches are illustrated and compared. 

We show that the use of a Taylor approximation in the derivation of 

the maximum entropy deconvolution filter allows an implementation much 

faster than conventional iterative techniques. The measured spectrum 

is modeled as the sum of a 2D random noise process and an ideal 

spectrum convolved with a generalized point spread function. Spectral 

lineshape parameters can be used to choose an appropriate point spread 

function. Once this convolution function is chosen, the 

resolutlon-enhanced spectrum can be rapidly reconstructed using the 

approximate form of the entropy in an iterative Newton-Raphson scheme.-- 

.. 

6 

AUTOMATED HI ~E~I'kA MADE ON AN XL-300: George S!omp. The Upjohn 

. . . 

Company, Kalamazoo, MI 49001 

An automated program for preparing routine IH spectra is described. The progra~ 

can run unattended saving much operator time, makes uniform spectra, and ~jnimizes 

human error. The program employs three levels of easily-modified MAGICAL "m macros and 

features" 

I. A wide variety of solvents are known and the program corrects for the 

ambiguous d7-DMF lock. 

2. Prompts ask for a title and other identification if desired. 

3. Escape is offered at potential trouble spots and resume is provided if manual 

interaction was taken. 

4. Current activity is always displayed. 

5. Output is identified with title, date, event time, method of referencing, 

ignored intense peaks and broad downfield lines. 

6. The f.i.d, is saved on a floppy. 

Spectra are referenced to ~.IS, solvent, or by default and then they are scaled 

vertically ignoring solvent, TMS, and unimportant intense lines. Threshold for the 

line list is offered at 3X noise level or if ignored it will iterate to a maximum of 

88 lines, or less for small molecules. The spectrum, integral, parameters, title, and 

other information are plotted on II x 17 blank paper using an HP7550 at a standard 

width of IOPPM. Broad downfield peaks are inset at left of plot. 

Potential troubles and their remedy will be illustrated. 

100

CALCULATION OF 2951MAS NMR CHEMICAL SHIFT FROM SILICATE 

MINERAL STRUCTURE: Sherriff, Barbara L. " and G:rundy H Douglas 

Department of Geology, McMasterUniversity, Hamilton, Ontario, L8S4MI... 

There have been many attempts to correlate 295i MAS nmr chemical shift 

with various parameters of silicate mineral structure. In our studies 

of mineral systems such as scapolites and Feldspars we Found these 

correlations to be inadequate For the interpretation of the complex nmr 

spectra. 

Silicate crystal structures were retrieved from a database and 

manipulated with a computer graphics modelling program• Further 

calculations revealed a simple correlation between 29Si MAS nmr 

chemical shift and molecular geometry that Is applicable to all 

silicate minerals. It is based on the magnetic anisotropy and valence 

of the bond between the terminal oxygen atoms of the silicate 

tetrahedron and the second nearest neighbour cation to the silicon. 

The correlation, which is based on 76 data points and has a 

correlationn coefficient of 0.911 with a standard deviation of 0.7ppm, 

can be used to calculate the chemical shift and hence to assess the 

validity of different structural models. 

X-ray diffraction methods can only determine the average of the 

AI-O and Si-O lengths for each tetrahedral (T) site in the case of 

minerals with AI-Si disorder. Comparison of measured chemical shifts 

with those calculated For structures with different T-O distances can 

give an estimate of AI content. 

8 NONLINEAR INCOHERENT SPECTROSCOPY 

J. Paff and B. BiOmich* 

Max-Planck-Institut fur Polymerforschung, 6500 Mainz, F.R. Germany 

In incoherent spectroscopy the Fourier transforms of the nonlinear 

cross-correlation functions of excitation and response are multidimen- 

sional spectra which correspond to the nonlinear susceptibilities. In 

stochastic NMR spectroscopy the Fourier transform of the cross-correla- 

tion algorithm has been applied in the past for the computation of 2D 

spectra in terms of 2D cross-sections through the 3D spectra of the 

third order nuclear magnetic susceptibility. 1 

We have tested the explicit time domain third order cross-correla- 

tion for the derivation of 2D cross-sections through the 3D time corre- 

lation function. After 2D FT one obtains z-COSY or exchange and MQ type 

2D spectra. This approach is of interest, since the evaluation can be 

executed in an analog fashion in parallel for each data point of the 2D 

time domain matrix. In this way the multiplex advantage may be introdu- 

ced to the additional dimension in 2D spectroscopy with the ultimate 

goal to measure a complete 2D spectrum within a few TI. The procedure is 

presently being implemented to obtain dead time free 2D ESR spectra, 

taking advantage of the low power of continuous stochastic excitation. 

The state of the art is described, and examples from NMR spectroscopy 

are given. 

i) B. BiOmich. Progr. NMR Spectrosc. 19, 331 (1987). 

101

ELIMINATION OF PHASE ROLL, SOLVENT SUPPRESSION, AND UNIFORM SPIN-1 

EXCITATION WITH SHAPED PULSES: Warren S. Warren, Mark McCoy and 

Andy Hasenfeld*, Department of Chemistry, Princeton University, 


We have recently shown that purely amplitude modulated or phase/amplitude modu- 

lated pulses can eliminate phase roll while exciting regions as narrow as 15 Hz; can 

produce undistorted two-dimensional spectra off resonance while completely eliminating 

the solvent peak; and can excite a broader quadrupolar powder pattern for the same 

amplifier peak power. All of these experiments were done with a slightly modified 

commercial spectrometer. Theoeretical work has uncovered a new infinite family of 

pulses with a rectangular excitation profile and complete insensitivity to r.f. field 

strength (similar to the (sech(~T)) I+5i pulses demonstrated by Silver), but the 

additional degrees of freedom permit improved phase characteristics and give new 

insight into the effects of pulse shaping. 

References: 

M. McCoy and W.S. Warren, Chem. Phys. Left. 133, 165 (1987). 

F. Loaiza, M. McCoy, S. Hammes and W.S. Warren, J. Mag. Res. (in press). 

A. Hasenfeld, Phys. Rev. Lett. (submitted). 

-- 

i0 

I 127I NMR STUDY OF QUADRUPOLAR ECHOES IN KI: B. C. Sanctuary, 

McGill University, Montreal, Quebec H3A 2K6. 

5 

The NMR observables of a system of single spin ~ nuclei can be described in terms 

k 

of the 2k-pole alignments population ~0 (i ~ k ¢ 5) and the q-th quantum coher- 

k k 

ences ~±q (k ~ q ~ 5, q ~ O), where the polarizations, ~q, are the expectation 

values of a set of k-th rank spherical tensor operators, or multlpoles. Theor- 

etical calculations are first given on the NMR spln-echo responses of this system, 

perturbed by a distribution of static electric quadrupole interactions, to various 

sequences of up to three intense r.f. pulse. Following this, we describe the 

results of some experiments on 127I in KI aimed at verifying these calculations 

and determining the relaxation behavior of the polarizations. 

102

AN NMR STUDY OF MISCIBLE BLENDS 

IN CONCENTRATED SOLUTION 

ii I *a b 

olly W. Crowther ,Israel Cabasso ,and George C. Levy Department 

of Chemistry, Syracuse University, Syracuse, New York, 13210 

acurrent Address- New Methods Research, Inc., 719 E. Genesee Street 

b Syracuse, New York, 13210 

Department of Chemistry, State University of New York-ESF 

Syracuse, New York, 13210 

High-resolution proton spectra of the miscible polymer blend 

polystyrene/poly(vinyl methyl ether) (PS/PVME) in concentrated 

solution have been used to examine intermolecular interactions. The 

spectral resolution achieved in solution allows the polymer components 

and the chemically different types of protons within each component to 

be well resolved. A one-dimensional cross-relaxation experiment shows 

that the polymers are intimately mixed in toluene solution but not in 

chloroform. The concentration threshold for observable magnetization 

exchange between the polymer pair (in toluene) lies between 30 and 40 

wt% total polymer, of which 50 wt% is polystyrene. The chemical shift 

difference between the methine and methoxy resonances of PVME is found 

to vary with the mole ratio of PVME to the total aromatic 

functionality, from either PS or toluene. Linewidth vs. temperature 

measurements seem to indicate hindrance of motion for the blend in 

toluene at elevated temperatures, as the gross phase separation is 

approached, that is not observed for the pure homopolymer. A 

two-dimensional exchange experiment was performed at a series of 

mixing times to measure the intra- and intermolecular spin-diffusion 

rates. Specific intermolecular rates could not be differentiated in 

the presence of the very fast intramolecular distribution of the 

_magnetization via_spin diffusion. 

[ 

~ 

POTENCY OF FLUORINATED ETHER ANESTHETICS CORRELATES WITH SPIN-SPIN 

RELAXATION TIME IN BRAIN: 

12 J D. Andre' d'Avfgnon 1. Joanna C. Haycock 2 and Alex S. Evers 2" 

Departments of Chemistry I and Anesthesiology 2, Washington University, St. Louis, MO 

631301 and 631102 . 

19F NMR signals arising from fluorinated anesthetics can readily be observed in 

brain tissue excised from anesthetized rats. When brain is suspended in D20-saline 

two anesthetic environments as characterized by different spin-spin (Tp) relaxation 

times can be observed I. The major anesthetic compartment (bound anesthetic) is highly 

immobilized (T 2 < 5 msec) while the minor component is believed in exchange with the 

aqueous phase (T 2 > 9 msec). The following observations are made: 

* T 2 times of the bound component for a variety of anesthetic ethers in brain correlate 

well with anesthetic potency as measured by ED50. Respective T2/EDso values 

are: Methoxyflurane, T 2 = 0.62 msec, ED50 = 0.0046 arm; isoflurane, T2-& 2.39, 

ED.^ = 0 016 arm; Enflurane, To = 2.90msec, ED.^ = 0.022 arm; fluroxene, T 2 = 4.30 

~U " ~ ~U 

ED50 = 0.035 arm. 

* Hexafluorethane, a non-anesthetic, shows a far greater T 2 time (18 msec) in brain 

than the anesthetics studied. Hexafluorethane partitions well into perinephric 

* 

adipose tissue and poorly into brain, suggesting low affinity for a binding site 

in brain. 

Anesthetics incorporated in adipose tissue show much longer T2's than in brain 

(200 - 400 msec) while hexafluorethane is 230 msec. 

Our conclusions from this work are: 

* The correlation of anesthetic potency with spin-spin relaxation time suggests 

anesthetics with highest binding affinity (greatest immobilization) are the most 

potent anesthetics. 

* Brain tissue contains b~nding sites for anesthetics which provide a markedly dif- 

ferent motional environment than sites found in adipose tissue. 

References: 1A~S. Evers et al. Nature 328, 157 (1987). 

103

- - QUANTIFICATION OF BLOOD FLoW AND TISSUE PERFUSION VIA DEUTERIUM 

13 I NMR-THE NOVEL USE OF D20 AS A FREELY DIFFUSIBLE TRACER: 

Joseph J.H. Ackerman 1" , Seong-Gi Kim I , Coleen S. Ewy I , Nancy N. 

5ecker I , Yuying C. Hwang I , and Robert A. Shalwitz2; Departments of Chemistry I and 

Pediatrics 2, Washington University, St. Louis, MO 631301 and 631102 . 

NMR has proven to be a valuable technique with which to monitor metabolic events 

nondestructively in intact biological systems. The past decade has witnessed dramatic 

advances in the development of such spectroscopic analyses employing 31p, 13C, and *H 

nuclides. Our laboratory has recently introduced a new approach, employing deuterium 

NMR in concert with D20 as a freely diffusible aqueous tracer, for the measurement of 

blood flow and tissue perfusion 1'2 This method borrows heavily from multicompart- 

ment kinetic modeling used with diffusible radiotracers such as H2150 and 133Xe but,of 

course, does not require the special handling procedures associated with radioactive 

labels. In addition, the deuterium NMR blood flow determination can be carried out 

concomitant with NMR metabolic analysis, thus, correlating in one measurement impaired 

substrate delivery and its physiologic consequences. In brief, the tissue or organ in 

which blood flow is to be determined is labeled with D20 via either intravenous, intra- 

arterial or intratissue bolus injection. Ongoing capillary blood flow, diffusion and 

proton-deuteron exchange serve to distribute HOD throughout the tissue's aqueous space. 

Further blood flow (unlabeled) then washes out the deuterium residue. The residue 

decay (washout) curve is accurately defined via external monitoring, i.e., 2H NMR. 

Single*, 2 and multicompartment modeling 3'4 and knowledge of the blood:tissue 

partition coefffcient (readily determined independently of the NMR residue decay curve~ 

allows derivation of blood flow and perfusion in units of ml-blood/(100 g-tissue,min). 

The extension of this method to NMR flow-imaging appears feasible s . [References: (i) 

J.J.H. Ackerman et al., Proc. Natl. Acad. Sci. USA, 84, 4099 (1987); (2) J.J.H. 

Ackerman e~ al., N.Y. Acad. Sci., 508, 89 (1987); (3) S.-G. Kim et al., Cancer 

Research, accepted (1987); (4) S.-G. Kim, et al., Magn. Reson. Med., submitted 

(1987); (5) C.S. Ewy eC al., Magn. Reson. Med., submitted (1987).] 

14 ] SILICON-29 MASNMR ANALYSIS OF SINTERED Si3N 4 CERAMICS: 

K. R. Carduner, Ford Motor Company, Dearborn, Michigan, 48121 

Silicon nitride is finding application in the transportation industry in 

various engine components such as valves, valve seats, or wrist pins that 

will operate with less wear and improved thermal characteristics compared 

to metal components. Gas turbine rotors constructed from Si3N 4 ceramic 

can operate at higher speeds and temperatures without the deformation or 

fatigue observed in turbines manufactured from high temperature alloys. 

Si3N 4 ceramics are made by conversion at high temperature of ~-Si3N 4 

precursor powder packed into a mold to ~-Si3N 4 into which is mixed 

approximately 5% of a "sintering aid" such as Y203 . The precursor powder 

must be mostly a-Si3N 4 and/or amorphous Si3N 4 phases and low in SiO 2 or 

Si2N20 for effective microstructure development during sintering. An NMR 

technique to analyze for phase purity in precursor powders has recently 

appeared (K. R. Carduner, e t al, Anal. Chem. 59, 2794, 1987). Presently, 

it is shown that NMR can provide insight into sintered ceramic as well. 

Test ceramics, which are not readily pulverizable, were machined into 

cylinders and inserted into alumina MAS rotors. 29Si MASNMR spectra can 

distinguish between the ~ and any residual ~-Si3N 4 phase, and it has also 

been possible to detect, assign resonances of, and quantify the grain 

boundary phases that result from reaction of yttria and Si3N 4. The grain 

boundary phases, which are at the level of i to 2 wt%, are often respon- 

sible for limiting the high temperature strength of Si3N 4 ceramics. 

Quantification of the grain boundary phases by other techniques are 

compared with the NMR results. NMR shows strong promise as a method to 

study crystalline versus amorphous morphology of the grain boundary 

pha~=s. 

104

15 II9F CRAMPS OF INORGANIC FLUORIDE COMPOUNDS: 

*Karen Ann Smith and Douglas P. Burum , Colgate-Palmolive, 909 River Road, 

Piscataway, NJ 08854, and Bruker Instruments, Inc., Manning Park, Billerica, 

MAOI821. 

The major mineral component of human dental enamel is hydroxyapatite. 

Fluoride treatment of apatite can result in formation of calcium fluoride 

and/or fluoroapatlte, depending on treatment conditions. In addition, 

dentifrices may contain various sodium or potassium salts which could result 

in a variety of fluoride-contalnlng compounds precipitating or forming. Many 

of these compounds have large fluorlne-fluorlne dipolar couplings, which 

broaden the spectra and ma~ resolution of individual resonances difficult 

with MASS alone. However F CRAMPS allows identification and resolution of 

calcium fluoride, fluoroapatite, sodium and potassium fluoride, and sodium 

and potassium monofluorophosphate, even when all are present simultaneously. 

Fluorine-19 has a large chemical shift range, which can be a problem in using 

multl-pulse techniques. Here, quad detection (achieved by data sampling in 

all 4 2~wlndows in the MRev-8 cycle and appropriate data manipulation) was 

used to double the effective sweep width of the multiple pulse sequence, and 

cover the range of chemical shifts needed. 

Spectra taken with 19F CRAMPS, as well as details of the pulse sequence and 

data handling used will be presented. 

16 I 13C NMR RELAXATION STUDIES OF GLUCONATE AND MANGANESE-GLUCONATE 

INTERACTIONS, W. Robert Carper* and David B. Coffin, Department of Chemistry, Wichita 

State University, Wichita, KS 67208. 

13 

The effect of temperature on the spin-lattice (R I) and spin-spin (Rp) C relaxa- 

tion rates of gluconate and manganese(II)-gluconate solutions is determined in D~O. 

We observe a R~ vs. temperature minimum for gluconate solutions similar to that ~b- 

served in solia-liquid phase transitions. Nuclear Overhauser enhancement factors 

indicate predominately dipolar relaxation mechanisms for all except the carbonyl 

carbon. Activation energies and chemical shifts indicate a molecular reorientation 

involving the carbonyl carbon which results in changes in solvation (hydrogen bond- 

ing) effects. Addition of manganese(II) to gluconate in D~O results in an observed 

temperature minimum in R 1 vs. reciprocal temperature plots for all except the carbonyl 

carbon atom. Activation energies further support the concept of changes in solvent- 

manganese-gluconate interactions affected by a change in intra-molecular structure. 

This work has been supported by a grant from NIDDKD (DK 38853). 

105

I~ 17 J QUANTITATIVE 2D NMR STUDIES OF PROTON EXCHANGE IN AMMONIUM ION. 

Charles L. Perrin and Tammy J. Dwyer,* Department of Chemistry, University-of 

California, San Diego, La Jolla, California 92093. 

To investigate kinetic isotope effects on proton exchange, we have studied 

ammonium ion by a combination of isotopic substitution and quantitative twodimensional 

NMR. Solutions of ISNHANO~ in a 3:2 mixture of D20:H20 result in five 

isotopomers of the ammonium ion, four of which are distinguishable in the IH NMR 

spectrum. At pH < 1 the protons exchange only with water. This is detected as 

crosspeaks connecting each isotopomer with its nearest neighbor(s). Base-catalyzed 

exchange involves transfer of a proton from an ammonium ion to an ammonia. In this 

case, crosspeaks are observed which connect the different spin states of the nitrogen 

nucleus as well as the individual isotopomers of the ammonium ion. It has been 

shown (Perrin and Gipe, J. Am. Chem. Soc. 1984, 106, 4036) that each crosspeak can 

be integrated to determine the site-to-site rate constants for the individual 

exchange processes. The rate constant for base-catalyzed proton exchange obtained 

by this method is 2.7 x 108 M -1 sec -1. This agrees nicely with a value obtained 

previously. More importantly, an isotope effect of kD/k H = 0.56 was observed for 

this process. 

18 J TWO-DIMENSIONAL NMR STUDIES OF THE CONFORMATIONS OF BRADYKININ IN 

AQUEOUS SOLUTION AND IN THE PRESENCE OF MICELLES: Susannie C. Lee and Anne F. 

Russell, Procter and Gamble Co., Miami Valley Laboratories, P.O. Box 398707, 

Cincinnati, Ohio 45239 

The conformational properties of a nonapeptide hormone, bradykinin, have been 

determined by two-dimensional NMR techniques at 500 MHz. In particular, homonuclear 

Hart_mann-Hahn (HOHAHA) and rotating frame cross-relaxation (ROESY) experiments were 

essential in the assignment of resonances and the elucidation of the structure of 

this 1280 Da polypeptide. Our studies indicate that bradykinin exists, in aqueous 

solution, either as a completely disordered structure or as an average of several 

conformations in fast exchange. To gain a better understanding of the structural 

properties of bradykinin in a cell membrane receptor environment, various micellar 

systems were examined for their ability to stabilize a preferred conformation. 

Three membrane mimetic systems were studied: sodium dodecyl sulfate (SDS), 

myristoyl-lysophosphatidyl choline, and dodecyl phosphocholine. The optimal system 

for this investigation was a mixture of bradykinin and sodium dodecyl sulfate 

(perdeuterated) at a 1:5 molar ratio, as confirmed by the temperature-dependent 

behavior of the amide protons. Under these conditions, we were able to detect the 

presence of a gamma turn at residues 7-9 of bradykinin. Detailed structural 

information, in the presence of SDS, was obtained from quantitative 2-D NOE analyses 

and distance geometry calculations. 

106

19 I DIPOLARAND SPIN-ROTATION POLARIZATION OF METHYL GROUP SPINS 

Michael Murphy and David White, Dept. of Chemistry 

University of Pennsylvania, Philadelphia, PA 19104 

We have investigated the proton NMR of molecules such as CH3CN , CH3CmCH , 

and CH3CI trapped at low concentrations in solid Kr. The methyl groups in 

these matrices undergo nearly free quantum rotation, allowing for polarization 

of methyl spins to occur via coupled spin and rotational relaxation following 

a temperature jump. Besides proton-proton dipolar polarization (the 'Haupt 

I 

effect' ), we have identified additional spin polarizations, namely, those 

associated with secular spin-rotation and heteronuclear dipolar interactions. 

Due to the magnetic isolation of the molecules, well-resolved powder line- 

shapes are obtained from which the contributions of different spin observables 

may be distinguished. We provide evidence that a finite spin-rotation cou- 

pling exists and determine the coupling constant for CH3CN/Kr by examining the 

signal component due to polarized 'spin-rotation magnetization'. Heteronuclear 

2 Is 

dipolar polarization is demonstrated in CH3CN/Kr. Lineshape analyses are 

shown to provide new information regarding the methyl group rotational levels. 

I. J. Haupt, Phys. Lett. 38A, 389 (1972); Z. Naturforsch 28a, 98 (1973) 

2. M. Murphy and D. White, J. Chem. Phys. 86, 1640 (1987) 

I -- 2 0 I NMR SIGNAL PROCESSING USING PADE APPROXIMANT AND LINEAR 

PREDICTION Z-TRANSFORM METHOD: J. Tang*, Y. Zeng and J. R. Norris, Chemistry Division, 

Argonne National Laboratory, Argonne, IL 60439 

Linear prediction (LP) theory has been widely applied to digital signal processing to overcome 

truncation and noise problems often encountered by the fast Fourier transform method. Here, a new 

approach 1 is proposed for NMR spectral analysis with enhanced resolution and sensitivity using Pad6 

rational approximation 2-s and linear prediction z-transform. 4 In the conventional LP methods 4 such as 

LPQRD or LPSVD, the whole spectrum is analyzed. In order to resolve all the spectral lines a very large 

LP filter length, usually several times that of the total number of spectral components, has to be used. 

In contrast, this method can be used to zoom into a small section of the whole spectrum for analysis if 

the spectral contents in some zones are of particular interest. Thus, this method uses a much shorter 

LP filter length and requires a smaller computer memory and shorter computational time. As LPQRD or 

LPSVD, this method also yields a table of spectral parameters without additional efforts required by FFT. 

Applications of this method and the comparisons with LPQRD or LPSVD will be presented. Other LP 

methods using computationally efficient autoregression (AR) or Burg algorithm s are particularly useful for 

2-D NMR signal processing. By LP extrapolation of the unobserved FID and application of line- 

narrowing apodization functions one can significantly improve spectral resolution while avoiding sinc- 

wiggling artifacts due to data truncation. 

. 

2. 

3. 

4. 

. 

J. Tang and J. R. Norris, Nature, (in press). 

E. Yeramian and P. Claverie, Nature 326, 169 (1987). 

J. Tang and J. R. Norris, J. Magn. Reson. (in press). 

J. Tang and J. R. Norris, in "Electronic Magnetic Resonance of the Solid State', Vol. 1, p. I11 

(1987) (Ed., J. Weil), The Canadian Society for Chemistry, Ottawa, Canada. 

J. Tang and J. R. Norris, Chem. Phys. Lett. 131, 252 (1986). 

This work was supported by the U.S. Department of Energy, Office of Basic Energy Sciences, 

Division of Chemical Sciences under contract W-31-109-Eng-38. 

107

21 DETECTION OF LONG-RANGE IH-19F COUPLINGS USING A HETERONUCLEAR 

[ EQUIVALENT OF THE COSY PULSE SEQUENCE. 

Donald W.Hughes and Alex D.Bain, Department of Chemistry, McMaster University, 

Hamilton, Ontario. Canada. LSS 4MI. 

Heteronuclear chemical shift correlation has become an indispensable technique for 

assigning the spectra of natural products. The original pulse sequence (I) 

IH : D1 - 90 ° - t I - 90 ° 

X : 90 ° - ACQ 

has been largely neglected by spectroscopists because of the complications arising from 

heteronuclear coupling in both dimensions. Recently this pulse sequence was reexamined 

with a phase-sensitive modification (2). The principle advantage this heteronuclear 

correlation (HETCOSY) method is that like the homonuclear COSY experiment it is a 

robust technique i.e.resistant to errors. HETCOSY can produce correlations between 

protons and X nuclei without prior knowledge of X-IH coupling constants. This feature 

makes HETCOSY useful for establishing correlations between protons and X nuclei such 

as 19F and 31p, especially in cases where the X-IH couplings are not well resolved. The 

present study deals with the application of HETCOSY in identifying which fluorine 

nuclei are responsible for long-range IH-19F couplings in corticosteriods related 

to fluocinonide. 

I. A.A.Maudsley and R.R. Ernst. Chem. Phys. Lett.50, 368 (1977) 

2. A.D. Bain. J. Magn. Reson. In press (1988) 

I -- 22 I 

STUDIES OF PHOSPHORYLATED SITES IN PROTEINS USING IH - 

David H. Live and Dale E. Edmondson # 

31p 

2-DIMENSIONAL NMR 

*Department of Chemistry and #Department of Biochemistry, Emory University, 

Atlanta, GA 30322 

The application of proton detected IH - 31p multiquantum 2-dimensional 

NMR to directly studying the phophorylated sites of proteins is demonstrated 

here. This approach works well for proteins up to molecular weight of about 40 

kD in spite of the fact ~at the 2D spectrum is mediated by small 3 or more 

bond couplings between ~P and protons on phosphorylated amino acid residues. 

Results are presented for the protein Azotobacter flavodoxin, an electron 

carrier in nitrogen fixation. The results provide the first direct evidence 

for the existence of a phosphate diester linkage between a seryl and a 

threonyl residue in the protein. Data from this protein are compared to that 

from phosphoserine, phosphothreonine and ovalbumin. 

108

2 3- I A SOLID-STATE 2H and 13C NMR STUDY OF THE STRUCTURE OF POLYANILINES: 

Samuel Kaplan* and Esther M. Conwell, Xerox Webster Research Center, 800 Phillips Rd. 011ll-39D, 

Webster, NY lt1580; Alan F. Richter and Alan G. MacDiarmid" Department of Chemistry, University of 

Permsylania" Philadelphia, PA 1910tl. 

Polyaniline, synthesized by the electrochemical or chemical oxidative polymerization of aniline, can 

exist as a number of unique structures of the form 

. . . . . ly~ . . . . . . x 

1A 2A 

where 0-

25 

-- I NUCLEAR MAGNETIC RESONANCE STUDIES OF GROUP VI METAL CARBONYLS ON 

OXIDE SUPPORTS: William M. Shirley, Department of Chemistry, Wichita State 

University, Wichita, Kansas 67208. 

High-resolution solid-state NMR has become an important technique for 

characterizing heterogeneous catalysts. In this study, 13C NMR was used to 

characterize surface species prepared by allowing Cr(CO)6 , Mo(CO)6 , and W(CO)6 to 

react with alumina and zeolite supports. Surface trlcarbonyl species, stable up to 

200°C for all three metals, have been observed by NMR on either y-alumlna or a NaX 

zeolite. The large downfleld shift of 247 ppm observed for Cr(CO)3/NaX indicates an 

anionic species. The molybdenum and tungsten carbonyls on alumina show a strong 

signal from an intermediate species with 4 or 5 CO llgands. Although diffuse 

reflectance visible spectroscopy indicates an intermediate species for the chromium 

carbonyl on the NaX zeolite, the NMR signal for this species is barely observable 

using maglc-angle spinning (MAS). Interpretation of MAS spectra in the presence or 

absence of cross polarization (CP) provides information on the mobility of surface 

species on alumina. While the spinning sldebands of the 13C resonance from 

Mo(CO)3/alumlna using CP/MAS indicate a very broad resonance (400 ppm), the 

intermediate carbonyl has a smaller chemical shift anlsotropy and is not enhanced by 

CP. The Mo(CO)3 species is apparently static while the intermediate species is 

rather mobile. Mobility is also indicated for Cr(CO)3/NaX since the resonance is 

only about 150 ppm wide. This resonance is narrow enough to be followed from a room 

temperature powder pattern to a relatively narrow llne above 150°C using a 

conventional liquids probe at 7 T. 

_ _ 

26 I A NOVEL METHOD FOR DETERMING ACTIVATION ENERGIES AND 

CORRELATION TIMES FROM NMR SPIN-LATTICE RELAXATION DATA 

Morton A. Fineman * 

Department of Physics 

San Diego State University 

San Diego,CA 92182 

The task of deducing the activation energies and correlation times from spin- 

lattice relaxation data consisting of relaxation time measurements at various 

temperatures at a fixed Larmor frequency has, in the past, been accomplished 

by employing complicated and tedious iterative programs. In this paper a novel 

technique is described which permits one to find accurate values of the activation 

energy and correlation times easily and quickly without the use of a computer. 

The only requirement is that a minimum value for the spin-lattice relaxation 

time is observed. A typical set of data from an NMR experiment on penta- 

deuterated ethane will be treated to demonstrate this method. Results 

obtained by this technique for several other compounds reported in the literature 

will be compared to the recorded literature values. 

The support of EE&G Incorporated , the US Federal Aviation Agency and 

the US Navy is gratefully acknowledged. 

110

27 1 COLLECTION OF PHOSPHORUS-31 NMR SPECTRA FROM RAT 

PUPS WITH INDUCED HYPERTHERMIA: Joseph J. Ford*, Katherine H. Taber 

and R. Nick Bryan, Baylor Magnetic Resonance Center, Houston, Texas 77030 

It is well known that hyperthermia in young animals will induce 

seizures, which involve the expenditure of a large amount of energy, and 

eventually death. Phosphorous-31 NMR can be used to monitor how seizures 

affect the levels of the high energy phosphorous metabolites. Measuring the 

phosphorous-31 NMR spectrum on a young, 5-20 day old, rat pup while 

inducing hyperthermia and monitoring the EEG presents a technical challenge. 

To collect the data, it was necessary to physically restrain the animal to 

insure that anesthetics not affect the results. There is very little free space 

inside the probe that is placed in the NMR magnet and the probe is at least 1 

foot inside the narrow (70 mm) cylinder of the NMR magnet. It was 

necessary to gently restrain the animal in this isolated, high magnetic field 

enviroment, while monitoring the EEG and internal body temperature, and 

adjusting the body temperature. A specially designed water blanket and a 

commercial thermocouple probe were used to monitor and maintain body 

temperture and the use of long lead electrodes enabled the collection of some 

EEG data while the animal was in the magnet. Evaluation of the equipment 

and techniques used will also be presented. 

-- 28 I HIGH PRESSURE DEUTERIUM SOLID STATE NMR OF POLYCRYSTALLINE CdPS 3 

I INTERCALATED WITH PYRIDINE: P. L. McDaniel, G. Liu and J. Jonas, University of 

Illinois, Urbana, IL 61801 

O O 

The use of the quadrupole echo sequence (90 -T-90 ) for the collection of 

• X. . 

deuterium powder pattern lineshapes which provzde inform~tzon about the dynamcs of 

the deuterated molecule is well known. We have applied this technique to the study 

of ds-pyridine intercalated into the VDW gap of the lamellar CdPS 3 host. Furthermore, 

we d~veloped a probe which allows us to study this system at pressures up to 4.5 kbar. 

Pressure experiments were performed for four isotherms, (270K, 300K, 330K and 

360K). Due to the absence of any large amplitude reorientational motion at 270K, 

pressure had a minimal effect on the lineshape. At 300K, 330K and 360K, however, 

increasing pressure results in a decrease in the VDW gap size which in turn has a 

marked effect on the reorienting pyridine molecule. Increasing pressure results in 

a reduction of the proportion of motionally reduced pyridine (a result of rapid 

reorientational motion of 3-fold or higher symmetry about an in-plane axis perpendi- 

cular to the molecular C 2 symmetry axis) to the rigid pyridine component. 

These high pressure deuteDium solid state NMR experiments show that an elevation 

in pressure produces lineshapes similar to those obtained with a decrease in 

temperature. These two methods of affecting intercalate dynamics are basically very 

different. Thermal expansion of the host material resulting in a larger VDW gap would 

be small. The application of pressure, however, results in an actual alteration of 

the VDW gap dimension. The use of high pressure to generate changes in the VDW gap 

could be useful in the simulation of the effect on intercalated molecules of similar 

host compounds whose differences lie only in their VDW gap size. 

111

2 ~ I SOLID-STATE NMR STUDY OF THE STRUCTURE AND 

DYNAMICS OF PLANT POLYESTERS AND INTACT PLANT CUTICLE. 

Joel R. Garbow', Tatyana Zlotnik-Mazori ~, Lisa M. Ferrantello ~ and Ruth E. Stark ~. . 

Life Sciences NMR Center, Monsanto Company, St. Louis, MO 63198 and #Department of 

Chemistry, College of Staten Island, City University of New York, Staten Island, NY 10301. 

Cutin and suberin are the structural polymers of plant cuticle, functioning in conjunction 

with lipid waxes and carbohydrate cell walls as effective barriers to the environment. In this 

poster, we report on a high-resolution solid-state 13C NMR study of these plant polyesters, 

designed to determine how their substituted fatty-acid constituents are linked together in 

a functionally useful way. Additional molecular information is derived from NMR analysis 

of cutin-wax and suberin-cell wall assemblies, as well as from solid residues remaining after 

partial depolymerization. 

Cross-polarization magic-angle spinning 13C NMR spectra with dipolar decoupling have 

been used to identify and quantitate the magnetically distinct carbons of these solid biopoly- 

mers. In samples for which a subset of the aliphatic carbons is sufficiently flexible to yield 

direct-polarization spectra with scalar decoupling, a quantitative comparison of immobile 

and mobile groups has been made. 13C and 1H spin-relaxation experiments (Tip(C), Tip(H) 

and TI(C)) have been used to probe polyester motions in the kHz and MHz frequency 

regimes, to examine crosslink structures that maintain cuticle integrity and to explore the 

nature of cutin-wax and suberin-cell wall interactions. 

-- 3o j 

A STATIC NMR IMAGE OF A ROTATING OBJECT 

S. Matsui,* K. Sekihara, H. Shiono, and H. Kohno 

Central Research Laboratory, Hitachi, Ltd. 

P.O. Box 2, Kokubunji, Tokyo 185, Japan 

An approach to imaging of a rotating object is described and demonstrated experimentally. 

The principle is to apply field gradients such that the NMR signal from the 

rotating object observed under the applied gradients results in appropriate scanning 

in the spatial frequency domain, or the k space. The scanning pattern must cover the 

k space as uniformly as possible. A static image of the rotating object can be obtained 

from such a scanning pattern by suitable data processing. 

When the whole object is moving, one must consider the field gradients in the 

moving object frame, 6 (t), (not in the laboratory frame, CR(t)). Then, the signal 

r 

scanning pattern in the object-frame k space is 

r 

r 

Here, D_ is a transformation depending on the object motion. In the case of rotation 

about t~e Y axis at an angular frequency(u s , D G is given by 

0 no/ 

D G = 0 s 1 st 

t 0 cos ~ t 

-sin ~s s 

In our preliminary two-dimensional (x,z) experiment, a gradient sequence in the 

laboratory frame, ~R(t) = (GoW t, 0, Go), was applied to obtain a spiral scanning 

pattern in the object frame, k ~t) = (~G~tsinw t, 0, ~G^tcos~ t). A phantom, 

r u U s 

consisting of two water-filled capillaries ~l.SSand 2 mm i.d.), was rotated at 180 

Hz. The obtained proton image was consistent with the dimensions of the phantom. 

112

31 DELAYED REFOCUSSING TWO-DIMENSIONAL NMR IN ROTATING SOLIDS 

A.C. Kolbert *'1'2, D.P. Raleigh 1'2, H.B. Levitt 2, R.G. Grlffin 2 

1 


and 

2 

Francis Bitter National Magnet Laboratory 

Massachusetts Institute of Technology 

Cambridge, HA 02139 

We describe a new class of two-dimenslonal MASS NHR experiments designed to 

measure small coupling tensors. The experiment, in its simplest form, involves 

the placement of a K-pulse at tl/2 after cross-polarizatlon, that is, in the 

middle of the evolution period, followed by unrestricted sampling during t~. 

The effect of the n-pulse is to delay rotational echo formation in t I resulting 

in the FID in t. having rotor echoes spaced at 2T . The 2-D spectrum resulting 

i 

from this experiment will have rotational sideban~s spaced at ~ /2 in the ~. 

dimension, while maintaining the effective spinning speed in ~2 ~ A further i 

example of experiments in this class is provided by an experiment which yields 

rotational sldebands at ~r/3 in ~I' and involves the placement of E-pulses at t 1 

and 2ti/3. 

32 

MEASUREMENTS OF TWO-DIMENSIONAL NMR POWDER PATTERNS IN ROTATING 

ISOLIDS.T. Nakal, J. Ashida and T • Terao* • Department ~ of Chemistr- y• 

Faculty of Science• Kyoto University, Kyoto 606• Japan. 

Switching-angle sample-spinnlng techniques for measuring the heteronuclear 

dipolar/chemical shift 2D powder patterns are reported. The techniques have the 

advantages of the high signal-to-noise ratio and the low distortion of the spectrum 

compared with those in stationary powder samples• Furthermore, for compounds with 

more than one chemically distinct nucleus• the individual 2D powder patterns can be 

separately obtained by 3D NMR. Practical applications of these techniques are 

demonstrated with the 13C 2D powder patterns of calcium formate, polyethylene, and 

polyacetylene. The chemical shift tensors and proton positions in calcium formate 

were obtained for the two crystallographically inequivalent formate ions, which 

agree with the results already reported by single crystal studies of 13C NMR and 

neutron diffraction. The chemical shift principal axes in polyethylene were found 

to be only approximately along the symmetry directions of the CH 2 group• indicating 

a strong perturbation of the electric environment by the crystal field• 

Current address: Department of Chemistry• University of California, Berkeley• 

CA 94720. 

113

33 

INTERPRETATION OF THE NMR NUTATION SPECTRA. A. Samoson* and E. 

I Lippmaa, Institute of Chemical Physics and Biophysics, Estonian 

Academy of Sciences, 200001Tallinn, USSR. 

The quadrupole interaction parameters of half integer spin nuclei are 

accessible from the dependence of NMR central transition signal on the rf excitation 

pulse length. The Fourier analysis yields (nutation) spectra, consisting at most 

of 21 major lines. The lines can be associated with single quantum coherences in a 

rotating magnetic field created by the rf pulse. The magnetization vectors 

describing spin evolution in the rotating magnetic field nutate in different senses, 

depending on the quantum numbers of respective energy levels. This provides for 

further unravelling of 2D spectra via hypercomplex Fourier transform. The ratio of 

a first moment to integral intensity of the nutation spectra gives a good estimate 

for the quadrupole interaction constant. The nutation spectroscopy applied to the 

study of zeolites, glasses and organic conductors provided for identification of 

various nuclear sites and interpretation of complicated ID spectra. 


CA 94720. 

34 I 

RF PUMPING EFFECTS IN HEXAMETHYLENETETRAMINE 

John P. Sanders *, Morton A. Fineman and Lowell J. Burnett 

Department of Physics, San Diego State University 

San Diego, CA 92182 

Couplings between the hydrogen and nitrogen nuclei in hexa- 

methylenetetramine (HMTA) produce weakly-allowed transitions at 

frequencies distinct from either the proton or the nitrogen Lar- 

mor frequencies. Pumping these weakly-allowed transitions with a 

CW rf source produces changes in the proton magnetization or, 

equivalently, in the apparent proton relaxation time, which are 

detectable by conventional pulse NMR techniques. 

In HMTA, significant effects were observed at rf pumping frequen- 

cies as far as 4.7 MHz away from the proton Larmor frequency of 

19.14 MHz. Evidence for a frequency-dependent structure in the 

response to rf pumping was also observed. Comparable effects 

were not observed for mannitol, a compound with similar proton 

relaxation properties that does not contain nitrogen. 

The support of EG&G Incorporated, the US Federal Aviation Agency 

and the US Navy is gratefully acknowledged. 

114

35 DYNAMIC NUCLEAR POLARIZATION STUDIES OF A MOLECULARLY 

DOPED POLYMER by Robert A. Wind, Liyun Li, and Gary E. Maciel, 

Department of Chemistry, Colorado State University, Fort Collins, CO 80523, 

Nicholas Zumbulyadis," Corporate Research Labora~ri~, Eastman Kodak 

Company, Rochester, NY 14650, and Ralph I-L Young, Copy Products Research and Development, 

Eastman Kodak Company, Roches~r, NY 14650. 

Small organic, charge-transporting molecules doped into inert polymer mal~ices offer many advantages 

as model systems for the study of elect~nic processes in amorphous materia~ We have studied 

samples of bisphenol-A-polycarbonate doped with various amounts of trianisylaml-lum percMorate 

and U~misylamine using pm~m DNP and C-13 DNP/CPMAS and DNP/HDMAS experiment~ The 

H DNP experiments indicam that the electron-proton interactious have both a time-independent and 

a ~ d e n t component. The former lead to enhancements due to the solid-stats and thermal 

mixing effects, the latter to an Overhauser enhancement. The Overhauser enhancement is positive, 

indicating that scalar electron-proton interactions dominat~ The addition of free amine reduces the 

proportion of Overhauser enhancement. 

The C-13 DNP/FIDMAS experimenm indicate differcntiat proton nuclear Overhauser enhancement as 

well as a mixture of solid-state, thermal mixing and Overhauser enhancement due to the unpaired 

• ele~mnL The implications of these obeervations for charge mobility and small molecu/e clustering 

in the polymeric matrix will be diwume& 

36 I 

FREQUENCY SWITCHED INVERSION PULSES AND THEIR APPLICATION TO 

BROADBAND DECOUPLING; Toshimichi Fujiwara and Kuniaki Nagayama 

Biometrology Lab, JEOL Ltd. Nakagami, Akishima, Tokyo 196, Japan 

First, the broadband inversion pulses with coherent 

frequency switching were designed. They are made of a few 

180°-like pulses which are different in frequency of about 

1.5 x B , where B indicates strength of r.f. field. The 

refined frequency differences and pulse widths were numerically 

searched under the constraint of symmetry about offset frequency. 

The operative frequency range of these pulses is about 

1.2 x B x n, where n is the number of frequencies used, or the 

number of 180 ° pulses in the sequence. Second, its performance 

and the tolerance to inhomogeneity of B field were improved by 

the phase cycling of 0 °, 150 ° , 60 ° , 150 ° , 0°. * Finally, 

decoupling pulse sequences were constructed from these improved 

inversion pulses using the phase cycle employed in MLEV-°4. The 

performance of these pulse sequences was experimentally tested, 

and theoretically evaluated with two scaling factors; J-scaling 

factor which characterizes the decoupling on a long time scale 

(long period scaling) and a scaling factor which characterizes 

the decoupling on a short time (short period scaling). 

*R.Tycko, A. Pines, Chem. Phys. Letters ll__!l, 462 (1984). 

115

37 IMOLECULAR MOTIONS IN SOLIDS MEASURED FROM 13C 

LINEWIDTHS: V. A. Nicely and P. M. Henrichs,* Eastman Kodak 

Company, Rochester, NY, 14650. 

We have found linewidths of the 13C resonances from solids 

to be a sensitive indicator of molecular motions. Often non-motional 

contributions to the linewidths obscure the motional linewideth due 

to motion in such cases. Fourier transformation of an entire echo 

train to give a spectrum broken into spikes (as demonstrated by 

Garroway and later by Zilm) is an efficient way to treat spin-echo 

results. The shapes of the individual spikes contain the information 

about motion. For examples spinning at the magic angle, the spacing 

of the echo pulses must be an integral multiple of the rotation 

period. Dimethyl sulfone, for which motions are well known, is a 

convenient test material. The linewidths are sensitive to both 

methyl rotations and reorientation of the_whole molecule. In polymer 

below the glass-transition temperature, -~C linewidths reflect the 

distribution of correlation times associated with local chain 

motions such as ring flips, methyl reorientations, and methylene 

oscillations. Results have been obtained from bisphenol-A 

polycarbonate, poly(ethylene terephthalate), and poly(ethylene 

isophthalate). This method is a useful way to probe motions in 

polymers and other materials for which isotopic labelling is not 

practical. 

38 HIGH RESOLUTION ELECTROPHORETIC NMR (ENMR) OF A MDflWJRE: 

Timothy R. Saarinen and Charles S. Johnson, Jr., University of North 

Carolina, Dept. of Chem., Chapel Hill, NC 27599-3290 

Electrophoretic mobilities have been measured in situ using 

pulsed field gradient NMR (PFGNMR). Several components in a mixture 

can be studied simultaneously by Fourier transformation of the second 

b~if of the spin echo. For a U-tube conficjuration application of an 

e!ectl'ic field across the sample results in a cosinusoidal modulation 

of spectral peak amplitudes, cos(Kv:t) where K equals the area of the 

gradient pulse times the gyrcmagnetic ratio, v is the drift velocity 

of the i'th species, and t is the duration of the electric field 

pulse. By working at low ionic strengths electric fields of up to 50 

V/cm could be applied for i sec before convection was detected by a 

change in the amplitude of the HOD peak. The cationic mobilities in 

a mixture of tetra-methyl and tetra-ethyl ammonium chloride in D.O 

were determined. Application of the technique for studying emu/sions 

looks prcnlising. 

116

I 

39 

2D NMR STUDIES AT 600 MHZ OF A PROTEIN-DNA COMPLEX USING IMPROVED TECHNIQUES 

FOR WATER SUPPRESSION AND HETERONUCLEAR CORRELATION SPECTROSCOPY 

C. OTTINC*, W. LEUPIN, A. EUCSTER, AND K. WOTHRICH, INSTITUT FOR 

MOLEKULARBIOLOCIE UND BIOPHYSIK, ETH, CH-8093 ZORICH 

The N-terminal DNA-binding domain 1-76 of the P22 c2 repressor was investigated 

in a I:I complex with a 16-base pair DNA duplex related to the ORI binding 

site. Starting from the sequence-specific resonance assignments previously 

established for the isolated protein and the DNA duplex, resonance assignments 

could be made for the complex using conventional 2D NMR techniques. For NOESY 

in H20 an improved scheme was developed which suppresses the water resonance 

without presaturation at the end of the mixing time, and provides uniform 

excitation in both dimensions, except for a region of approximately +/-1.5 ppm 

in ~2 centered about the water line. To obtain simplified IH-NMR spectra of the 

complex, a protein preparation with 15N enriched lysine and arginine residues 

was prepared. The resonances of the protons directly bound to 15N were then 

selectively observed using 15N(~ 2) half-filtered NOESY. IH- detected 15 N 

correlation spectroscopy was performed using the pulse sequence by Bodenhausen 

and Ruben (Chem. Phys. Lett. 69, 185 (1980)). To record [IH,15N]-COSY spectra 

the performance of the experiment was improved by insertion of short spin lock 

pulses which purge all undesired signals originating from protons not directly 

bound to 15N. The purge pulses enabled us to use this experiment also for 

[IH,13C]-COSY at natural abundance with a 5mM solution of repressor 1-76, and 

to extend the pulse sequence with a TOCSY-type mixing period to obtain relayed 

correlations. 

~ ALTERNATIVE METHODS FOR COLLECTION OF 2D-NMR SPECTRA: Peter 

40 I Rinaldi* and Dan Iverson+, Department of Chemistry, The 

University of Akron, Akron, OH 44325* and Varian Instruments, 611 Hansen Way, 

Palo Alto, CA 94303+. 

The standard method for obtaining 2D-NMR spectra involves collection of 

all NT transients at a single evolution time before incrementing tl, where NT 

is an integral multiple of cycles such as CYCLOPS to systematically reduce ar- 

tifacts, and n is the number of t I increments. 

(90x-O-90x-AT)NT, (90x-0-90y-AT)NT, (90x-T-9Ox-AT)NT, 

(90x-T-90y-AT)NT, (90x-2T-9Ox-AT)NT, (90x-2T-90y-AT)NT, 

.... (90x-nT-90x-AT)NT, (90x-nT-9Oy-AT)N T 

When magnetization is not permitted to fully decay (as is typically the 

case) this method produces systematic t I artifacts such as the characteristic 

"false" COSY crosspeaks that appear from sharp singlets. Alternative orders 

for collection of 2D-NMR data have been examined using the COSY sequence. 

Collection of a single transient for all values of t I and repeating the se- 

quence NT times provides considerably better artifact suppression and at the 

same time requires fewer steady state cycles if NT is small. 

[(90x-0-90x-AT), (90x-T-9Ox-AT), (90x-2T-90x-AT), 

.... (90x-nT-9Ox-AT), (90x-0-90y-AT), 

(90x-T-9Oy-AT), (90x-2T-90y-AT) .... , (90x-nT-90y-AT)]NT 

Sample data obtained from trans-stilbene and methy methacrylate are 

shown to illustrate the level of artifact reduction. 

117

41 

A HYPO-RELAXATION AGENT; SIMULTANEOUS USE WITH HYPER-RELAXATION 

AGENTS TO IMPROVE LOCALIZED CONTRAST IN NMR IMAGING. 

Jonathan P. Lee * 

Department of Diagnostic Radiology 

The New England Deaconess Hospital and Harvard Medical School 

There are at least six types of i~rac~ions which can contribute to spin- 

lattice (Tl) relaxation in NMR of solutionsl The relative difference in the 

amount thaf any specific interaction contributes to the total relaxation rate 

at discrete locations is believed to be a major contributing factor in image 

contrast. So called "contrast agents" (CAs) act in part by increasing the 

contribution of paramagnetic interaction to the rate of T 1 relaxation. While 

the relative difference between T 1 relaxation at discrete locations is increased, 

it can be argued that there is an overall decrease in the potential dynamic 

range for image contrast. 

If one were to decrease the contribution of another type of interaction 

which contributes to T I relaxation, and furthermore be able to simultaneously 

effect spatial localization between this decrease and the increase observed 

from CAs, then it follows that the potential dynamic range of image contrast 

would be extended. In practice this would "push" one location's T] up, and 

another's down, thus extending in both directions the relative differences in 

T I relaxation and thereby the relative image contrast. 

I. Becker, Edwin D.; in High Resolution NMR, Academic Press, 1980. 

4 9 

] 

l Sequence-specific H NMR Assignments for Cobrotoxin 

Chin Yu*, Chi-Yina ~Jano 

Chemistry Department , National Tsing Hua University, Hsinchu, Taiwan 

Cobrotoxin is a neurotoxic protein isolated from the venom of 

Taiwan cobra (Naja naja atra). This protein, which blocks the 

neuromuscular transmission at the post-synaptic membrane by the 

specific binding to the acetylcholine receptors, contains 62 amino 

acid residues (Mr 6949) with four disulfide brid~es. 

The assignment of the IH NIIR spectr~n at 30°C of cobrotoxin is 

described and ducumented. The assignments are based entirely on the 

amino acid sequence, phase-sensitive homonuclear 2D NMR experiments, 

idenfication of complete spin systems, NOEs, and studies of pH 

dependence of NMR spectrum on 400 MHz. 

118

43 

Coherent Averaging Theory Under the Condition of Strong 

P, dses o4 Finite Width and Its Application 

Wu Xiaoling, Zhang Shanmin , and Wu Xuewen 

Department of Physics, East China Normal University, 

Shanghai 200062, P.R.China 

Abstract 

A theory, Coherent Averaging Theory Under the Condition of 

Strong Pulses of Finite Width, is presented by using perturbation 

method of quantum mechanics combining with Coherent Averaging 

Theory. It is proved that under the condition of strong pulse, 

i.e. when the interaction coupled with RF field , ~I , is 

stronger than the internal interaction among spins themselves, 

~;nt , by a factor of more than six , instead of the whole ~ 

only the secular part in ~i~t with respect to ~1 , which 

commutes with ~1 , needs to be remained during the pulse° 

Compared with the method commonly used to deal with pulses 

with finite width, this technique is of much more convenient 

and of little lower degree of approximation in the applications. 

Some applications of this method in various experiments are 

discussed. Especially, equipped with this technique , we have 

designed a windowless solid echo pulse sequence and a solid 

state broadband composite 180 ° pulse, which are superior to 

those scheme~generally utilized. 

119

-- 

I 44 

TWO DIMENSIONAL LINEAR PREDICTION NMR SPECTROSCOPY 

] • 

Henrik Gesmar and Jens J. Led 

University of Copenhagen, Dept. of Chemical Physics 

The H.C. 8rsted Institute, 5, Universitetsparken 

DK-2100 Copenhagen, Denmark. 

Linear prediction has been introduced into the field of NMR spectroscopy as a valu- 

able method of quantitative spectral estimation (1,2). Its applicability has been de- 

monstrated even in case of broad band spectra with many narrowly spaced resonances (3), 

i.e. cases where LSQ curve fitting procedures (4) would seem to be unfeasible. 

In the present study it is demonstrated that the application of the linear predic- 

tion principle can be extended to include two dimensional N!IR spectroscopy, without 

increasing the computation time drastically. 

Examples are presented and the advantages as well as the pitfalls of the procedure 

are discussed. 

(I) H. Barkhuijsen, R. de Beer, W.M.M.Jo Bov6e, and D. van Ormondt, 

J. !.lag n. Reson. 6_~I, 465 (1985). 

(2) J. Tang, C.P. Lin, M.K. Bov~nan, and J.R. Norris, J_. ~agn. Reson. 6_22, 167 (1985). 

(3) H. Gesmar and J.J. Led, J. !4agn. Reson. (1988). In press. 

(4) F. Abildgaard, H. Gesmar, and J.J. Led, J. Magn. Reson. (1988). In press. 

45 I INTERGLYCOSIDIC 13C_I H COUPLING CONSTANTS. AN APPROACH TO 

D ACCHARIDE AND POLYSACCHARIDE CONFORMATIONS. C. Morat, LEDSS, University of Grenoble 

R.F. Taravel, CERMAV-CNRS: F38402 Saint Martin d'Heres FRANCE. 

Interglycosidic C-H coupling constants have been measured for different 

disaccharides (methyl B-cellobioside, methyl B-maltoside, octa-O acetyl B-gentiobiose 

methyl B-isomaltoside, B-D-mannobiose) and one oolysaccharide (5-3-6 triacetyl 

cellulose) in natural abundance by the selective 2D-J heteronuclear exoeriment. 

Their values give access to the torsion angle of the glycosidic link when used in 

conjunction with a KARPLUS-tyDe relationship. 

120

46 

CARBON-13 SPECTRAL ASSIGNMENTS OF DNA OLIGOMERS: APPLICATIONS OF PROTON-DETECTED 

HETERONUCLEAR 2D-NMR: J. Ashcroft*, and D. Cowbum, The Rockefeller Univ., New York, New York, 10021-6399 

Heteronuclear multi.spin coherence proton detected chemical shift correlated NMR (HMP-COSY), may be 

used to obtain 2D IH-{13C} correlated spectra. Carbon resonances can then be assigned via NOESY and COSY derived 

proton assignnmnts. Proton-carbon correlated spectra can also provide useful information without supplementation. In 

the 1D proton spectxum of DNA oligomers, the resonances arising from the 1', 3', 4', 5' and the cytidine H5 protons all 

occur within an approximam.ly 2 ppm wide region, while in the 1D carbon spectra these groups, except the 1' and 4' are 

well separated. In the 1H-{tJC} correlated spectrum all groups are distinct, and.group assignments are greatly facilitated. 

Proton and .cybon chemical shifts, along with single-bond coupling constants (zJcH obtaided in the HMP-COSY experi- 

ment when laC decoupfing is not appfied during acquisition), can be used to assign resonances to a specific type of 

nucleotide residue. For example, the adenine C2 and the cytidine C5 chemical shifts are unique, enabling identification of 

these resonances. Also, the purine base CH pairs exhibit IJcrl'S at least 30 Hz. greater than pyrimidine base CH pairs. 

The I-IMP-COSY experiment uses a mixing period of duration 1/2./, to ensure maximum coherence transfer 

between proton and carbon. For single-bond coupling, this value ranges from 2.5 msec. to 4.0 msec., (J = 125 to 200 

Hz.). If the mixing period is between 40 and 100 msec., the HMP-COSY experiment is optimized for multiple bond cou- 

piing, (J = 12.5 to 5 Hz.). In such an experiment one can obtain a proton-carbon correlated spectra, which contains 

proton-non-protonated carbon cross peaks. Thus, assignment of carbonyl and quaternary carbons is possible. 

In principle the above two methods can be used to assign all carbon resonances in a DNA duplex. For practi- 

cal reasons,-- extreme spectral crowding, cancellation of anti-phase peaks, and complications of spectral interpretation due 

to strong-coupling,-- the 2', 2" and 5' carbon resonances can not be fully assigned using these techniques. The use of 

proton-detected IH-{IH-13C}-RELAY experiments to obtain the 2', 2" and 5' carbon assignments is examined. 

The effectiveness of different pulse sequences used to obtain IH-{13C} I-IMP-COSY spectra are compared. 

Examples obtained from the study of the duplexes d(TAGCGCTA)2, d(GGTATACC)2 , d(GGAATTCC)2 , are shown. 

Supported by grants from NSF, NIH, and the Keck Foundation 

121

A New Model for Hartmann-Hahn 

Cross Relaxation in NI,iR 

Wu Xiaoling , Zhang Shanmin and Wu Xuewen 

Department of Physics, East China Normal University, 

Shanghai 200062, P.R.China 

Ab s tract 

It was found out for the first time that Hartmann-I{ahn 

cross relaxation between rare and abundant spins in IZ~.~ proceeds 

in two stages: first, a fast energy exchange between each rare 

spin S and its directly bonded I spins, and then, a much slower 

one between these SI subsystems and remaining I spins. During 

n 

the cross relaxation, especially in the first stage, the I spin 

system is not always in a quasiequilibrium state and so is not 

always describable by a single temperature. 

122

a 

b 

48 

SEMUT SPECTRAL EDITING, CALIBRATION OF RF FIELD STRENGTHS, AND 

TOSS AT HIGH SPINNING SPEEDS IN 13C CPIMAS NMR OF SOLIDS 

N.C.Nielsen *a, H.Bildsee a, H.J.Jakobsen a, and O.W. Ssrensen b 

Department of Chemistry, University of Aarhus, DK-8000 Aarhus C, Denmark 

Laboratorium fur Physikalische Chemie, ETH, CH-8092 Zurich, Switzerland 

Pulse techniques for spectral editing have become popular tools for assign- 

ment of liquid state 13C NMR spectra. This work describes ~xtension of the con- 

cept of spectral editing to include 1D and 2D SEMUT editing of 13C CP/MAS NMR 

spectra for solids. Furthermore, as solid state NMR multipulse experiments are 

extremely sensitive to missetting of pulse timings we also report a 2D CP/MAS 

pulse sequence for fast and accurate calibration of rf field strengths. The se- 

quences are based on principles known from ID and 2D NMR experiments of liquids 

combined with techniques for obtaining high-resolution NMR spectra of solids. 

Finally, we present new and improved four and six ~-pulse TOSS sequences for ef- 

ficient suppression of spinning sidebands under various experimental condi- 

tions. Compared to earlier sequences the new TOSS schemes are advantageous for 

high-speed MAS experiments, for samples with short T2's, or for efficient dipo- 

lar dephasing of protonated carbons in 13C CP/MAS NMR at high speeds. Experimen- 

tal results obtained using our new sequences will be presented. 

49 * I CHEMICAL SHIFT IMAGING OF HUMAN INTERNAL ORGANS AT 1.5T 

William J. Thoma , June S. Taylor, Sarah J. Nelson and Truman R. Brown. 

Fox Chase Cancer Center, Philadelphia, PA 19111 

For NMR spectroscopy to be clinically useful, the sensitivity, quantification and 

volume localization must be optimized. Sensitivity is a function of field strength, 

homogeneity and rf coll design, quantification can be a~hieved by post-acquisitlon 

processing. We have implemented chemical shift imaging (CSI) on a 1.5T Siemens 

Magnetom (clinical imager) to localize volumes of interest. The simplest method of 

localization is to combine a I-D version of CSI with a surface coll to achieve 3-D 

localization. Localized signal is obtained by spin excitation by a non-selectlve rf 

pulse from the surface coil followed by an incremented phase-encodlng gradient pulse of 

3.1 msec duration. The ADC is turned on immediately after the rf pulse; data obtained 

during the gradient-on time is zeroed before fourier transformation. The technique has 

been used to obtain heart and liver spectra (Figure la, b, respectively) in 8 min. The 

spectra were obtained with a i0 cm, 2 turn surface coll and were from 1.5 and 1.0 cm 

thick slices, respectively. The repetition time was i sec with the pulse amplitude 

adjusted to produce a nominal 90 ° pulse in the region of interest. 3-D CSI sequences 

~ve also been implemented. 

T.R. Brown, B.M. Kincaid and K. Ugurbil. PNAS 79, 3523 (1982). 

Figure i. 

123

-- 50 I PIQABLE: AUTOMATIC AND RELIABLE QUANTIFICATION OF LOW SIGNAL TO 

NOISE SPECTRA. Sarah J. Nelson and Truman R. Brown, Fox Chase Cancer Center, 

Philadelphia, PA 

Interpretation of the results of in vivo spectroscopy requires a rapid, unbiased and 

reproducible method for quantifying low signal to noise spectra. Typically, these 

spectra have variable baseline, a variety of peak shapes and some partially overlapping 

peaks. We have recently developed a technique which performs peak identification, 

quantification and automatic baseline estimation (hence PIQABLE) for such spectra. The 

original version of PIQABLE was calibrated on simulated spectra (Nelson and Brown, 

1987). We have now refined the algorithms to include the options of automatically 

estimating phase correction parameters and of detecting and estimating areas of 

partially overlapping peaks. The accuracy of these refinements has been examined on 

simulated data which have peak signal to noise ratios in the range I00:I to 3:1. The 

parameter values and error estimates which PIQABLE provides are accurate to within the 

limitations imposed by the random noise. The new version of PIQABLE has been applied 

to a wide range of experimental data, including human calf, liver, heart and brain. 

Because the analysis is automated, it has proved particularly useful for application to 

situations where multiple spectra are collected such as kinetic data or chemical shift 

imaging data. 

-- 51 I SOLID STATE NMR INVESTIGATIONS OF CERAMICS AND GLASSES 

WITH EXTREMELY LONG SP•IN-LATTICE RELAY~TION TIMES: T. E. Hammond*, 

R. D. Boyer, J. R. Mooney, BP America Research & Development, Cleveland, 

Ohio 44128. 

Several inorganic ceramics and glasses have been studied by solid state 

N~[R which have been found to have extremely long spim-lattice relaxation 

times. These materials are typically void of hydrogens. Therefore, 

single pulse, Bloch decay-experiments are usually the only method which 

can be used to acquire an NMR spectrum. Included in these studie~ have 

been the C-13 and Si-29 spectra of alpha silicon carbide, Si-29 spectrum 

of silicon sulfide glasses, and the Y-89 spectrum of yttrium oxides. 

The worst case appears to be for certain compositions of the silicon 

sulfide glass, where the Si-29 T I can be on the order of 15-25 hours. 

The silicon carbide appears to have a di,tribution of T.'s, ranging from 

several seconds to over a thouoand seconds. In the SiC case, it is beiieved 

that metal impurities provide paramagnetic sites that induce relaxation 

of neighboring silicon atoms. Since there are no abundant spin active 

nuclei present, spin diffusion is not a possible mechanism to induce 

relaxation of those silicon atoms removed from the paramagnetic centers. 

Yttrium Tl'S appear to be on the order of 200-1500 seconds for several 

yttrium compounds studied. 

124

'--- V 5 2 j INTERCONWERSION OF VALENCE TAUTO~RS IN 

CYCLOBUTADIENE-LIC.~ [NAN &RGON MATRIX 

~ Onmd~ B. P,. Arnold, J. G. Radziszewski, J. C. FaceUi, IC D. Malsch, H. Sumb, D. lvL Crank and J. Michl 

Department of C3~¢mistry, Univer;ity of Utah, Sail Lake City, Utah 84112 

The static 13C ]qMR dipolar spectrum of cyclobutadiene in an argon matrix is ~ . Vicinal]y 13C labeled 

cyclobutadiene was generated photochemically fzom 1,2-13C2-cyclobutene-3,4.dJcart~xylic anhydride which wa 

diluted in argon at a matrix ratio of about I:I00. 

0 

13 248 nm 13 

"--"--- .,. • CO . C02 

Ar 13 

13 25K A 13 

o B 

Dipolar spectra of the p~'ursor, cyclobutadiene, and the dimer of cyclobutadiem were at] obtained. 

Previous matrix isolation polarized IR specm)scopy results indicate that cyclobutadiene is either rotating in th( 

matrix and/or interconverting between its two tautomers, A and B. Spectral mmuladons of the expected pauem for 

the above cas~ as we].l as for the case of a nonmta~g noninterconverting molecule were completed. "Fnese simu.la- 

fioas show that there is interconversion between the two valence mummers, A and B,which is at least comparable to 

53 I 

NMR CHEMICAL SHIFT ASSIGNMENTS BY ISOLATION OF 

MOLECULAR CONFORMATIONS IN SOLUTION AT LOW TEMPERATURES. 

PLATINUM- PHOSPHINE COMPLEXES: L. A. Luck*, C. H. 

Bushweller, A. L. Rheingold, Department of Chemistry, 

University of Vermont, Burlington, Vermont 05404 

31p{IH} DNMR has been used to probe the stereodynamics of a series 

of [(t-C~Hg:~2PR]2PtCl complexes. (R= CH3, C6H5, C6HsCH2, C2H5) In all 

cases, below 150K, the spectra indicate as many as four sub-spectra (4 

conformations). Assignment of the NMR peaks to specific conformations 

has in the past been speculative. This poster will show how we solved 

the dilemma. We will show how X-ray crystallographic data in 

conjunction with isolation of specific conformations in solution at low 

temperatures allowed unequivocal assignment of 31p{IH} NMR signals to 

specific conformations. 

125

s4 IA 13C CP/MAS AND 2H WIDELINE VARIABLE TEMPERA- 

TURE STUDY OF BECLOMETHASONE DIPROPIONATE--HEXANE IN- 

CLUSION COMPLEX: Thomas A. Early1-* and Mohindar S. Puar§, ~GE NMR 

Instruments, Fremont, Califorina 94539 §Schering-Plough Corp., Bloomfield, 

New Jersey 07003 

A solid inclusion complex, beclomethasone dipropionate--hexane, has 

been previously studied by magic angle spinning NMR methods 1. The complex 

presents an interesting system for CP/MAS study because of the wide range of 

motions present. For example, even though the hexane methyl reorients at a rate 

consistent with liquid-like tumbling, the hexane carbons easily cross polarize. 

When the hexane guest molecule is deuterated, and wideline dueterium 

spectra are obtained at a variety of temperatures ranging from 100 ° C to below 

-160 ° C, lowering the sample temperature results in an unexpected narrowing of 

2H Pake powder pattern resonances of the hexane-d]4 guest molecule. This in- 

teresting temperature behavior leads to models that 13C CP/MAS can distinguish. 

1 "Carbon-13 Nuclear Magnetic Resonance Studies of a Solid Inclusion Com- 

plex", T.A. Early, J.F. Haw, A. Bax, G.E. Maciel, and M.S. Puar, The Journal of 

Physical Chemistry, 88, 324(1984). 

SS 

I 

HUMAN IN VIVO SPECTROSCOPY AT 4.0T 

Dietmar Hentschel, Jurgen Vetter, Ralf Ladebeck, and Michael J. AIbright* 

Siemens AG, D-8520 Erlangen, FDG 

A 4 T six-coil SCM with a warm bore of 1.25 m diameter was designed 

with high homogeneity for use with in vivo spectroscopy. Computer optimized 

design was used to correct terms up to 10th order. The magnet can be ramped 

to 4 T in 1 hour. The rated current is 376 A, and the stored field energy is 39 

MJ. The field drift is less than 3.6 x 10-8/h, and bare homogeneity of 100 ppm 

can be corrected to less than +2.5 ppm for a 50 cm dsv. The total magnet 

weight is 10.6 tons. 

Increased spectral dispersion will be shown by comparison with 2 T 

spectra. Human in vivo 31p spectra at 4 T show resolution of the different 

PDE resonances, and, on some spectra, separation of the dinucleotides and 

nucleoside diphosphosugars upfield of the (z-ATP peak. 

High field RF penetration will be demonstrated with a 1H image at 4 T. 

126

[ 

~ THE SOURCE OF AN ARTIFACT IN THE IH - IH DECOUPLED 

$6 I HETERONUCLEAR CHEMICAL SHIFT CORRELATION EXPERIMENT 

Alex D • Bain* , Donald W. Hughes, Dept. of Chemistry, McMaster University, 

Hamilton, Ontario, Canada LBS 4MI; and Howard N. Hunter, National 

Research Council of Canada, Biotechnology Research Institute, Montreal, 

Quebec, Canada H4P 2R2. 

When the IH - IH decoupled variation of the heteronuclear 

two-dimensional chemical shift correlation experiment (shown below) is 

applied to methylene groups with inequivalent protons, a strong artifact 

may show up at the average chemical shift of the two protons. The 

artifact does not appear to be a strong coupling effect, since it appears 

in methylene groups with large proton chemical shift differences• 

However, it behaves apparently erratically with respect to the shift 

difference. Simulations with the SIMPLTN program indicated a strong 

dependence on the delay D2 in the sequence, and this led to a full 

explanation. The mechanism for this artifact is presented, along with 

experimental confirmation. 

90 90 180 90 

,H ~-] t,/2 ~ t,/2 

I 3 C 

180 

V- 

90 

io2 

90 

F7 

: ACQUIRE 

57 I STRUCTURAL STUDIES OF LIPIDS IN FIELD ORDERED MODEL 

MEMBRANES: Preetha Ram*, Maureen P. O'Brien* and J. H. 

Prestegard, Department of Chemistry, Yale Un.iversity, New Haven, 

CT 06511 

. . . . . . . . . . . ° 

Oriented, as opposed to randomly dispersed samples of 

biological membranes . o~ model membranes offer unusual 

opportunities for structural characteriztion. Quadrupole 

splittings in deuterium NMR spectra can, for example, be resolved 

in multiply labelled compounds and interpreted in terms of 

preferred orientation relative to membrane surfaces. In the past 

most methods for obtaining oriented samples have relied on 

mechanical orientation. More recently magnetic field ordered 

systems have been developed. We compare data on two types of 

magnetic field ordered micelles: potassium laurate and bile 

salt/dimyristoylphosphatidylcholine with phospholipid bilayers 

mechanically oriented on glass plates. The physical 

characteristics of these systems are investigated using 

quadrupole splittings from deuterium NMR and Carbon-13 

dipolar couplings obtained from Magic Angle Spinning experiments. 

Methods are presented for obtaining structural data on 

conformational aspects of specifically labelled lipids and lipid 

like molecules such as phosphatidylcholine, myristic acid and a 

galactose terminal lipid. Resulting quadrupole coupling data are 

merged with molecular energetics information derived from a 

molecular mechanics program to determine probable geometry at the 

bilayer interface. 

127

$8 I 

MEASUREMENT OF T I RELAXATION RATES OF COUPLED SPINS VIA 2D ACCORDION 

SPECTROSCOPY WITH APPLICATION TO ACYL CARRIER PROTEIN 

Lewis E. Kay*, Anne F. Frederick*, and James H. Prestegard 

Department of Chemistry, Yale University, New Haven, CT 06511 

Nuclear magnetic resonance spectroscopy (NMR) is widely recognized as 

a useful technique for probing dynamic and structural properties of 

macromolecules. Analysis is most commonly approached through measurements 

of NOE spectra. However, the same I/r 6 distance dependence that makes NOE 

spectra useful in assessing structure enters into spin-lattice or T 1 

relaxation times. In principle, T 1 recoveries can be used for structural 

analyses. Application of conventional ID NMR techniques or use of 

information on the diagonal in 2D experiments is often impossible due to 

lack of spectral resolution, and recently proposed combinations of 

inversion recovery experiments with two dimensional COSY detection (IR- 

COSY) are very time consuming. 

We have developed a pulse sequence based on the accordion experiment, 

which provides a framework for the reduction of the time consuming three 

dimensional IR-COSY experiment to a more practical 2D experiment. We will 

present applications of this sequence to the measurement of IH TlS in Acyl 

Carrier Protein (ACP), a small protein of molecular weight 8800 D. IH TlS 

obtained from a sample of ACP in the absence of metal and in the presence 

of Mn 2+ have been used as constraints in molecular mechanics calculations 

in order to locate the metal binding sites in this protein. 

59 UNTRUNCATIO.~I OF DIPOLE-DIPOLE COUPLINGS IN SOLIDS, OR ZEP, O FIELD 

I NMR ENTIRELY IN HIGH FIELD. Robert Tycko, AT&T Bell Laboratories, 

Murray Hill, NJ, 07974. 

N;:R spectra of powdered or noncrystalline solids in high field commonly exhibit broad 

lines that arise from the dependence of the nuclear magnetic dipole-dipole couplings 

on molecular orientation. New experiments will be described in which that orientation 

dependence is removed by the combination of rapid sample rotation with a synchronized 

rf pulse sequence. The sample rotation and pulse sequence have the effect of con- 

verting the usual truncated dipole-dipole couplings into an untruncated form. The 

result is N~IR spectra with sharp lines and splittings that depend only on inter- 

nuclear distances, i.e. spectra with a "zero field" appearance that are obtained 

entirely in high field. Such spectra provide a means of studying molecular conforma- 

tions in solids without requiring single crystals. The theory behind untruncation 

experiments will be presented along with experimental spectra of simple organic 

solids. 

128

60 

GLUCOSE METABOLISM IN PERFUSED HEARTS MONITORED BY 

I13C NMR SPECTROSCOPY: A MORE SENSITIVE INDICATOR OF 

ALTERED FLOW THAN HIGH ENERGY PHOSPHATE LEVELS. 

V. P. Chacko*, R. G. Weiss, J. D. Glickson and G. Gerstenblith 

The Johns Hopkins Medical Institutions, 600 N. Wolfe St., Baltimore, MD 21205 

Cardiac metabolism was studied in the intact, beating, perfused rat heart using 

13C NMR Spectroscopy and correlated with function and 31p NMR assessment of high 

energy phosphates, inorganic phosphate, and cellular pH during normal (15 ml/min) 

and graded reductions (5 ml/min & 2 ml/min) in coronary flow. Despite a 50% mean 

reduction in developed pressure at 5 ml/min flow, there was no change in levels of 

PCr, ATP, Pi or pH throughout the 60 minute period. There were, however, marked 

metabolic changes detected by 13C NMR monitoring levels of glutamate and lactate. 

These changes were not due to decreased delivery of glucose during low flow, as 

matched reductions in delivery achieved by lowering perfusate glucose during normal 

flow did not reproduce the low flow profile. The results are consistent with an 

increased dependence on anaerobic metabolism, and a reduction in tricarboxylic acid 

cycle flux during low flow. A delayed time to half maximum enrichment of the C2 

glutamate peak, but not the increased lactate levels, could be produced by 

decreasing workload to match that present during low flow by decreasing perfusate 

calcium concentration, indicating a close relationship between workload and this 13C 

NMR index of TCA flux. Further reduction in flow to 2 ml/minute resulted in further 

delay in the time to half maximum enrichment of C2 glutamate isotopomer, higher 

livels of lactate, as well as the classical "ischemic" changes in the 31p NMR 

spectra. Thus, 13C NMR spectroscopy can be used to characterize metabolic changes 

during reduced flow and altered workloads and is more sensitive than 31p NMR 

spectroscopy in identifying hypofunctional myocardium in which modest flow (supply) 

reductions are accompanied by a balanced down-regulated workload (demand). 

6~ ] Cu NQR OF YBa2CusO x WITH VARYING OXYGEN CONTENT: 

A. J. Vega*, W. E. Farneth, R. K. Bordia, and E. M. McCarron, Central 

Research and Development Department, E. I. du Pont de Nemours and 

Company, Experimental Station, Wilmington, Delaware 19898. 

The 63Cu and 6SCu NQR spectra of YBasCusO x show a strong dependence 

on the oxygen content when x is varied from 6 to 7. For x=7 two 

signals are observed at room temperature. The room-temperature 

signals generally consist of a short-T 1 (< 1 ms) and a long-T 1 

component (~ 100 ms). The relative intensity of the short-T I 

component gradually decreases from 100% to 0% when x is decreased 

from 7.0 to 6.0. In addition, the line shapes of the two T 1 

components are strongly dependent on the oxygen content. While the 

short Tl'S are attributed to a Korringa-type relaxation mechanism 

involving the conduction electrons, it may be assumed that the Cu 

sites with the longer T 1 values are not directly associated with the 

conduction process. The NQR data can thus be used to help interpret 

the strong dependence of T c on the oxygen content of these 

superconducting materials. 

129

MEASUREMENT OF 13C-15N DIPOLAR COUPLINGS IN SOLIDS 

62 J 

Vincent Bork*, Terry Gullion, Andy Hing, and Jacob Schaefer 

Washington University, St. Louis, Missouri 

The 13C-15N dipolar coupling in solids is measured directly 

in 2D double-window Dipolar Rotational Spin Echo (DRSE) 

experiments utilizing either an odd or even number of = pulses 

after the first rotor period. Inserting a ~ pulse into both 

carbon and nitrogen channels is equivalent to leaving both out in 

the even double-window C-N DRSE experiment. An odd double-window 

DRSE experiment involves using just one • pulse, which can be 

placed in either the carbon or nitrogen channel. The net C-N 

dephasing in the even double-window experiment after one complete 

rotor period of dipolar modulation is zero, and its resulting 

dipolar powder pattern is indistinguishable from that observed in 

a single window DRSE experiment. In contrast, net dephasing 

occurs throughout the dipolar evolution period of the odd 

double-window experiment because 

the single ~ pulse reverses the 

sign of the C-N dipolar j 

interaction. The dipolar H ~ DEOOUPLE 

modulation period is thus twice 

O-N DIPOLAR MODULATION 

the rotor period, and the c ~ ~ i ~=~"~ 

resulting Fourier transform 

reveals a new powder pattern with N ~ r ~ ~ = _ _ _ ~ _ _ _ _ 

dipolar sidebands at intervals of 

half the rotor frequency, rotor I I I 

63 I EFFECT OF 15N PULSE SPACINGS ON 13C-15N REDOR 

TERRY GULLION* and JACOB SCHAEFER 

Dept. of Chemistry, Washington Univ., St. Louis, MO 63130 

Manipulation of the 13C-15N dipolar interaction in a rotational 

echo double resonance (REDOR) experiment can lead to a major 

reduction in amplitude of 13C rotational echos. (The basic REDOR 

experiment will be presented in the Monday Morning Session on 

Magic Angle Sample Spinning.) The REDOR experiment produces a 

13 C- 15 N dipolar interacti o n that has a non-zero average over each 

rotor period. The location of the ~ pulses during each rotor 

cycle, and the number of rotor cycles during which the ~ pulses 

are applied, both affect this average. For example, a string of 

pulses spaced by one-third of a rotor period (TR/3) produces 

full rotational echos, whereas a string of ~ pulses placed at 

Tr/3,Tr,4Tr/3,2Tr, 7TR/3,3Tr, .... produces almost complete 

destruction of the 13C rotational echos. In addition, while the 

amplitudes of the rotational 

echos initially decrease 

with the first few cycles, 

amplitudes of the residual 

echos oscillate with 

increasing number of rotor 

cycles. 

__J 

H ~ CP 

REDOR 

DECOUPLE 

7~ 

N 

,30 root I I I I

. °- F 

64 I 

MICROSCOPIC IMAGING OF LIVE MOUSE AT 400 MHz 

Susanta K. Sarkar*, Russell Greig and Mark Mattingly' 

Smith K1ine & French Laboratories, King of Prussia, PA 19406-0939, and 

'Bruker Instruments, Billerica, MA, 01821 

The development of NMR microscopy is potentially useful in determining 

the fine structure of pathological lesions, and in particular in monitoring 

the growth and spread of malignant tumors in small animals. However, since 

the signal to noise ratio is the key limitation for imaging experiments with 

microscopic resolution, it is necessary to do these experiments at higher 

field strength. 

He demonstrate here the feasibility of obtaining live mouse images with a 

resolution of lOOxlOOx650 I~m at 400 MHz. Examples wtll tnclude images of 

human tumor xenografts tn nude mtce and mouse kidney. A wide bore Bruker 400 

MHz NMR spectrometer, modified for imaging experiments, was used for these 

experiments. 

65 I 

APPLICATION OF A ONE DIMENSIONAL IMAGING EXPERIMENT= 

Babul Borah, Norwich Eaton Pharmaceuticals, Inc., Norwich, NY 13815 and 

Nikolaus M. Szeverenyi, SUNY Health Science Center, Syracuse, NY 13210 

Although the trend has been towards increasing complexity in imaging experiments, 

we have found a useful application for a one dimensional imaging experiment in quan- 

tifying and characterizing the fluid changes in the rat leg as a result of arthritis. 

A large rf probe is used to insure that BI is uniform in the region of the rat 

leg and a single linear magnetic field gradient is applied continuously in the di- 

rection of the leg. A spin echo pulse sequence provides a signal which maps the 

spatial distribution of water and fat along the leg. In order to make quantitative 

measurements on the leg, a reference capsule containing water is placed Just beyond 

the paw. TI and T2 measurements can be obtained using the same techniques as in 

spectroscopy and suggest that there are two fluid components which are sensitive to 

infl-,,,atory soft tissue changes. One component has a T2 of 34 ms and the other 120 

ms. These components increase in concentration by a factor of 3 and 7 respectively 

as the lesion of the Joint progresses and appear to peak in 15-20 days after the 

induction of the arthritis in the rat. 

131

- - 

i 

66 

NMR IMAGING TECHNIQUES IN MATERIALS SCIENCE 

Simon Chu* and David Foxall. 

Spectroscopy Imaging Systems, Fremont, CA 94538. 

We have used NMR imaging as a non-destructive tool to monitor transition and diffusion 

between liquid and solid phases in a number of different practical examples. A major problem 

associated with imaging techniqes to date is a lack of ability to quantify fundamental physical 

parameters. We have paid strict attention to the problem of obtaining quantitative results from 

NMR images. 

Adhesives, resins and piasters provide practical examples of systems undergoing 

solidification by different mechanisms, which include condensation reaction (silicone glue), 

evaporation of solvent (plastic wood filler) and hydration of water (plaster). The 

methanol/polymethyl methacrylate system is an example of liquid permeation into solids, of 

practical significance in aircraft windshields. Water/agarose provides a controlled model system 

for diffusion studies. 

We will present results of these systems in the form of imaging time course studies and 

analysis to obtain kinetic data and diffusion coefficients. A disscusion of the problems 

encountered in making our measurements and how we have attempted to overcome them should 

provide some insight into how NMR imaging can be used in materials science studies. 

67 

Ramanathan, 

Philadelphia, 

I 

DEVELOPMENTS IN NITROGEN-14 NMR SPECTROSCOPY: R. McNamara, K.V. 

and S.J. Opella, Department of Chemsitry, University of Pennsylvania, 

Pennsylvania 19104 

Recent results which extend the utility of nitrogen-14 NMR spectroscopy will 

be presented. The experiments involve measurement of relaxation parameters of 

model peptides over a range of temperatures down to liquid helium temperaturs and 

of nitrogen-carbon dipolar couplings. For example, t4N overtone decoupling results 

in simplification of 13C spectra and helps as an additional assignment tool leading to 

structure determination. Two-dimensional NMR experiments that enable 

measurement of carbon-nitrogen, dipolar couplings will be presented. The 14N 

relaxation data will be discussed in terms of possible sensitivity enhancement at low 

temperatures and other applications such as 14N spin exchange experiments. 

132

68 

69 

CONFORMATIONAL ANALYSIS via 

VICINAL CARBON-HYDROGEN COUPLING 

Andrew L. Waterhouse 

Chemistry Department, Tulane University 

New Orleans, LA 70118 

The Fully Coupled (FUP) Correlation Experiment has been used to analyze 

conformation and stereochemistry on two dissimilar compounds, strychnine 

and camphor. The FUP experiment detects the vicinal coupling between 

hydrogeus and carbons, and the magnitude of this coupling is appraised by 

the presence or absence of cross-peaks in the spectrum plot. This corre- 

lates with a first-order approximation Of the Karplus torsional angle- 

relationship. The FUP experiment works better than other similar methods 

that detect vicinal C-H coupling because it has no J-filters to alter the 

signal intensity of the coupling. 

VECTOR GRAPHICS TO DEPICT MULTIPULSE NMR 

Andrew L. Waterhouse 

Shawn P. Garbett 

Department of Chemistry, Tulane University 

New Orleans, Louisiana 70118 

An educational program which graphically presents the vector diagrams 

often used in explaining multipulse NMR is written for the Commodore 

Amiga. It greatly enhances the clarity of the vector explanations as one 

can actually see vectors refocus. "Experiments can be entered with up to 

three independent signals, each of which can be coupled to 0-3 

independent nuclei. While the experiment is being run, the vectors are 

displayed in three dimensions, and ~e pulse sequence is shown with the 

current time point indicated. The presentation can be interrupted at any 

point. Presentation of a lesson can be done interactively or selected 

experiments can be easily recorded on standard videotape for later 

playback. Copies of the program are available. 

133

70 I 2H NMR STUDIES OF MOTIONS IN SOLID D2S AND D2Se: 

M.J. Collins, C.I. Ratcliffe,* and J.A. Ripmeester, Chemistry Division, 

Research Council of Canada, Ottawa, Ontario, Canada KIA OR9 

National 

There have been a number of tH and 2H NMR studies of motions in the three solid phases 

of H2S. There are, however, a number of ambiguities concerning these results, and the 

also yield little insight into the nature of the motion in phase II. The current work 

mainly concerns 2H powder lineshapes of D2S as a function of temperature. New work on 

phase II of D2Se is also included, since the behaviour appears similar to that of D2S 

phase II. In phase III of D2S close to the phase transition the lineshapes indicate 

the onset of a motion which is best explained as 180" flips, though other alternatives 

suggested by earlier IH T I_ results will be discussed. To be compatible with 

dielectric results this motion must be about the dipole axis of the molecule. Phase I 

of D 25 and D2Se proved to be much more interesting. The narrowed lineshapes indicate 

an axially symmetric motion in the fast motion limit, over the whole temperature range 

of phase II, but the averaged quadrupole coupling constant decreases substantially as 

the temperature increases. This suggests a fast motion for which angular parameters 

are varying as a function of T. Although a unique motion cannot be assigned possible 

models will be presented. 

71 ] STUDIES OF FLAVODOXIN BY HOMONUCLEAR AND 

HETERONUCLEAR 2D NMR TECHNIQUES. V. Thanabal* & Gerhard Wagner, 

Biophysics Research Division, Institute of Science and Technology, University 

of Michigan, Ann Arbor, MI 48109 

Most studies of protein conformations by NMR have concentrated so far on molecules of 

molecular masses below 10 kDalton. We have approached assignments of flavodoxin from 

Megasphaera elsdenii which has a molecular weight of 15 kDahon (137 residues). Although the 

classical 2D NMR pulse sequences (COSY, NOESY, RELAY) yielded satisfactory spectra we 

have heavily used TOCSY (HOHAHA) spectra and heteronuclear techniques for characterization of 

the amino acid spin systems. Compared to COSY and RELAY experiments these techniques suffer 

much less from cancellation of antiphase cross peaks due to a large linewidth. TOCSY spectra 

were recorded with an MLEV17 spin lock as described by Bax and Davis. Experiments with 

different mixing times were used to obtain a complete set of connectivities. Heteronuclear 1H-13C 

COSY experiments were recorded either with a heteronuclear multiple quantum evolution period or 

with a double DEPT editing sequence to separate CH, CH2 and CH3 carbons. The purpose of the 

heteronuclear experiments was mainly to elucidate the spin systems of the coupled protons. First 

sequential assignments obtained with these techniques will be presented. 

A.Bax and D.G.Davis J. Magn. Reson. 65, 355-360 (1985). 

134

72 I 

SCUBA, A MAY TOHARDS COMPLETE IH SPECTRA IN PROTEINS, AND EFFICIENT USE OF 

15N LABELS IN PROTEINS. 

Luciano Mueller*, Paul L. Heber and Stephen C. Brown 

Smith Kline & French Laboratories 

Research & Development Division 

P.O. Box 1539 

King of Prussia, Pennsylvania 19406-0939 

A common problem in proton NMR experiments performed in H20 solution is 

the loss of resonances associated with CH saturation of the solvent peak. Two 

recently developed tricks help to alleviate the problem. I. Huthrich and 

coworkers proposed to precede 2D sequences with a homonuclear mixing block 

(TOCSY, HOHAHA) to remagnetize the saturated HC=-peaks in proteins. 2. He 

proposed a method based on N0E type cross-relation (SCUBA=SCheme w£th 

Unprecedented Bad Acronym) which is claimed to be more efficient than TOCSY. 

Details of SCUBA, which allows protons to breath under water, will be 

presented. 

The combination of proton-nigrogen-15 chemical shift correlation with 

TOCSY, COSY and NOESY appears to be a powerful tool to sort out ambiguities 

caused by severe resonance overlaps in proteins. Experimental realizations of 

these methods will be presented together with software which aids and 

automates analysis of heteronuclear spectra. 

73 1 

THE AUTOMATED NMR LABORATORY 

by 

Stephen G. Spanton, Peter Fruehan and Richard L. Stephens* 

Department of Analytical Research, Abbott Laboratories 

North Chicago, IL 60064 

The integration of an NMR spectrometer with a robotic workstation and 

an external computer network provides a~l efficient means of preparing and 

acquiring spectra of l~rge numbers of NMR samples. In the system being 

developed at Abbott, a chemist identifies his sample to a computer network. 

The computer returns a barcode label which is put on the sample vial. 

The robot subsequently reads the barcode, identifying the sample, adds the 

previously specified solvent, filters and transfers the solution to an NMR 

tube, and inserts the sample into the spectrometer magnet. The computer 

system then downloads appropriate commands to the spectrometer which 

executes the desired experiment. The resulting data file is transfered to the 

computer network where it is numbered, entered into a database, archived, 

Fourier transformed and sent to the plotter nearest the submitting chemist. 

135

74 

PH EFFECTS ON THE SOLUTION CONFORMATION OF 

SHIKIMATE-3-PHOSPHATE: DETERMINATION BY NMR AND 

DISTANCE GEOMETRY CALCULATIONS. 

Stephen Castellino*, Gregory C. Leo and R. Doug Sammons 

Monsanto Agricultural Company, A Unit of Monsanto Company, 

800 N. Lindbergh Boulevard, St. Louis, Missouri 63167 

The solution structure was determined for shikimate-3-phosphate (S3P), a cyclohexenyl 

sugar derivative which is a metabolite in aromatic biosynthesis. Nuclear Overhauser effects (NOE) 

and coupling constants were measured as a function of solution pH. The preferred conformation 

found experimentally is the pseudo-axial chair with the 3-phosphate occupying an axial position. 

This agrees with the conformation determined by force field calculations (MM-2). Comparisons of 

experimental and theoretical three dimensional structures will be shown as a function of pH. 

7s I 

ASSIGNMENTS OF 31p AND IH RESONANCES IN OLIGONUCLEOTIDES BY TWO DIMENSIONAL 

HETERONUCLEAR HARTMANN-HAHN SPECTROSCOPY. M.G. Zagorski*, M.W. Kalnik, X.Gao, 

D. Norman, and M. Kouchakdjian, Department of Biochemistry and Molecular 

Biophysics, College of Physicians and Surgeons, Columbia University, New York, 

New York 10032, USA. 

A modified he~eronuc~ar 2D shift correlation experiment is demonstrated 

for assignment of H and P resonances in a variety of DNA olig~ucleotides 

ranging in size from a self-complementar~1octamer (seven unique P atoms) up to 

a complementary nonamer (sixteen unique J~P atoms). The modified pulse scheme 

incorporates a MLEV-17 composite pulse scheme for achieving net magnetization 

transfer among protons via a homonuclear Hartmann-Hahn (HOHAHA) type cross 

polarization. This net homonuclear magnetization transfer is then relayed to 

the --P atoms via an INEPT sequence and consequently recorded and processed to 

provide high quality pure phase absorption spectra via the hypercomplex method. 

Despite the relatively broad lin~ of these large DNA sequences, we were able to 

unambiguously assign all of the -~P resonances and many of the C-I', C-2', C-4' 

and C-5' sugar protons. These assignments were greatly facilitated by the 

presence of rel~ cross peaks spanning 4 and 5 bonds from the C-I' and C-2' 

protons to the --P nuclei. This relayed system removed many ambiguities present 

from overlap of the C-3', C-4' and C-5' resonances. Although the experiment 

described here does not provide the gains in sensitivity of the heteronuclear 

multiple quantum coherence (indirect) experiments, it clearly provides an order 

of magnitude improvement in sensitivity and resolution over ~her currently 

available methods for (direct) detecting the less sensitive --P nuclei. 

136

76 

NMR CHARACTERIZATION OF THE 

GLYPHOSATE-SHIKIMATE-3-PHOSPHATE- ENZYME 

DEAD-END COMPLEX. 

Stephen Castellino, Gregory C. Leo', R. Douglas Sammons and James A. 

Sikorski 

Monsanto Agriculture Company, a Unit of Monsanto Company, .800 N. 

Lindbergh Boulevard, St. Louis, MO 63167 

The herbicidal dead-end ternary complex of glyphosate with EPSP syn- 

thase (EC 2.5.1.19 from E. toll) and the substrate shikimate-3-phosphate 

(S3P) has been characterized by 13C,1S N and 31p .NMR. The enzyme bound 

glyphosate and S3P have unique chemical shifts. The phosphorus chemical 

shifts observed for glyphosate are shown to be dependent upon the position 

of the phosphorus atom relative to the free electrons of the nitrogen atom. 

77 I 

PULSE SHAPING AND SELECTIVE 

EXCITATION : THE EFFECT OF SCALAR COUPLING 

R. Bazzo0, J. Boyd and N. Soffe, Dept. of Biochemistry, 

University of Oxford, Oxford, UK. 

Recently, a good deal of interest has centred around the 

use of shaped pulses for a variety of ID and 2D experiments. 

Long low power rectansular pulses or waWeforms shaped like 

Hyperbolic Secants, Sine: func.tions, Oaussian or half- 

Gaussian functions have been used in these experiments. 

For very seleotlve pulses the averase r.f. power is 

adjusted to be the same order of masnltude as the J 

couplin S. A theoretical description suitable for sele,=:tive 

shaped pulses is siven, which includes the effect of the 

scalar couplin 6. The excitation profile for the different 

coherence components of the irradiated spin will be shown 

for the commonly used shaped waveforms. 

137

PHOSPHATE PLASTICIZER DYNAMICS IN GLASSY POLYMER BLENDS BY 3~F~ CSA 

-- LINESHAPES: Paul T. Inglefield*, Alan A. Jones, Ajoy K. Roy and 

I 78 IBonnie J. Cauley (Department of Chemistry, Clark University, 

Worcester, MA 01610) and Roger P. Kambour (Polymer Physics and Engineering, General 

Electric Company, Research and Development Center, Schenectady, NY 12301) 

The ability of 3tp CSA lineshape collapse to critically determine subtle details of 

the microscopic dynamics in the solid state is presented. The particular example of 

the motion of phosphorus containing diluents in solid polymer blends is considered. 

No sub-glass transition mechanical loss peaks are observed in 50:50 blends of poly 

(2,6-dimethyl-1,4-phenylene oxide) and polystyrene. However if organic phosphate, 

)lasticizing diluents (e.g. trioctyl phosphate) are added, the modulus is lowered and 

a broad low temperature loss peak appears. Non-spinning 3Xp lineshapes were observed 

and clearly indicate the onset of plasticizer motion in the glass. An axially symme- 

tric lineshape at low temperature evolves to a narrow line below the glass transition. 

At intermediate temperatures a superficially bimodal lineshape is observed indicative 

of a broad distribution of correlation times. The plasticizer motion appears to be 

isotropic in nature and detailed quantification of the dynamics is possible. The dy- 

namics of different phosphate diluents correlates with the glass transition of the 

pure diluent and it is postulated that the plasticizer motion is responsible for the 

low temperature mechanical relaxation. 

7 9 I NON UNIFORM SAMPLING IN NMR EXPERIMENTS 

Y. Manassen and G. Navon*, School of Chemistry, Tel Aviv University, 

Ramat Aviv, Tel Aviv 69978, Israel. 

In many NMR experiments the resonance frequencies and the 

linewidths are known a-priory and only the peak intensities are sought. 

This includes spectroscopic imaging experiments and 2-D NMR experiments 

(such as COSY and NOESY), where the possible frequencies of the peaks 

and their approximate linewidths can be obtained from the 1-D spectrum. 

It is shown here that a significant improvement in sensitivity can be 

obtained in such cases by collecting the data in a non-uniform manner 

instead of constant dwell times. It is further shown how the error in the 

intensity calculation can be estimated, and how this can be used to select 

the sampling times so that the the sensitivity is maximized. The increase 

in sensitivity is particularly pronounced in cases with small number of 

peaks and in cases where the distribution of the peaks in the spectrum is 

non-uniform. Our simulation experiments indicate that the calculated 

amplitudes are not very sensitive to errors in the linewidths. 

138

8o I 

HIGH RESOLUTION MR IMAGING AT 4.7T OF THE CENTRAL NERVOUS SYSTEM 

IN RATS: Paul C. Wang, Alan Muraki, Sunder Rajan, Charles 

Wambabe, Alessandro Guidotti, Mark Carvlin, Georgetown 

University, Washington, DC 20007. 

The rat is used commonly as an animal model in neurological 

research. One of the inherent problems has been to discern 

extremely small structures and detect pathological changes in the 

rat's brain. High resolution in vivo nuclear magnetic resonance 

images of the brain and spinal cord in rats were obtained using a 

4.7 Tesla magnet with a 33 cm bore imaging system (Spectroscopy 

Imaging System, Fremont, CA). Detailed anatomic structures are 

revealed due to the high resolving capability (resolution: ]20 um 

x 120 um, 4 averages). The slice thickness was 1.5 mm. A 2- 

Gauss/cm gradient coil with a 2-inch diameter saddle shaped RF 

coil was used. The RF coil was connected to the matching and 

running circuit by means of a 50~ transmission cable. Standard 

spin warp techniques with TR range from 0.3 sec to 3.0 sec and TE 

range from 22 msec to 50 msec were utilized to obtain the TI and 

T2 weighted images. Detailed microscopic structures such as the 

basal ganglia, ventricular system, and olfactory bulb as well as 

defining the gray matter from the white matter are clearly shown. 

In vivo relaxation times of the brain tissue at 4.7 Tesla were 

also measured. 

81 J SODIUM IMAGING OF OCULAR TUMORS: Susan J. Kohler *,a, Nancy H. Kolodnyb, c, 

and Swarna Balasubramaniam b, aBrigham and Womens Hospital, Boston MA 02115; bWellesley 

College, Wellesley MA 02181; CMassachusetts Eye and Ear Infirmary, Boston MA 02114 

Operating at field strengths of 1.5 and 1.9 T, we have developed 23Na magnetic resonance 

imaging protocols which provide high resolution multi-echo sodium images in short times. Using 

rapidly switchable gradients with minimum eddy currents we have implemented a multi-echo gradient 

echo technique (J. Granot, J. Magn. Reson. 68, 575 (1986)) which produces acomplete three- 

dimensional set of useable ocular images with 2x2x2mm voxels in four minutes by co-adding eight 

echoes (TE=3.5ms). Alternatively, longer acquisition times may be used, and the echoes processed 

individually to yield eight T2-weighted image sets. Since the echo time is only 3.5 ms, T2*'s may be 

readily calculated. 

Enucleated human and bovine eyes have been studied by these techniques. Conditions including 

intraocular tumor, retinal detachment, and vitreous hemorrhage have been clearly visualized in these 

systems. We have developed procedures to allow voxel by voxel calculations of T2 ° values from the 

eight echoes generated from the gradient echo technique we employ. At 1.9 T the T2 ° value measured 

from saline solutions is approximately 55 ms. The addition of increasing concentrations of 

Tris3DyTTHA shift reagent shortens the T2* values as expected, reaching a value of 8.5 ms for a 

solution containing 0.75 M NaCI and 0.05 M shift reagent. The measurement of T2* in the vitreous of 

enucleated bovine eyes is more difficult due to increased noise, but preliminary results indicate T2* 

values on the order of 50 ms. 

Related studies of the "visibility" of sodium in the bovine vitreous have provided the 

interesting and provocative result that the sodium in this environment has a visibility of 

approximately 80%. This value is intermediate between the 100% visibility predicted for sodium in 

an isotropic environment and the 40% visibility predicted for sodium in an anisotropic environment, 

and is suggestive of two sodium pools within the vitreous. 

139

82 

BROADBAND PULSES FOR EXCITATION AND INVERSION IN I=i 

SYSTEMS 

D.P. Raleigh*, E.T. Olejniczak 2 and R.G. Griffin 

Massachusetts Institute of Technology, Cambridge, MA 02139 U.S.A.; 

2Abbott Park Laboratories, North Chicago, IL 60046. 

New composite pulses for exciting and inverting three-level systems 

are presented. The n/2-pulse is designed for use in quadrupole echo 

spectroscopy and has a bandwidth comparable to existing sequences and 

is slightly shorter. Two new broadband n-pulses are presented which 

have bandwidths larger than other existing I=I inverting pulses without 

being significantly longer. The composite n-pulses have bandwidths 

exceeding + 2m .. Experimental examples and numerical calculations are 

presented ~hic~ldemonstrate the usefulness of these sequences. 

83 

I 

DEUTERIUM NATURAL ABUNDANCE NMR SPECTROSCOPY: 

MONOTERPENE BIOSYNTHESIS, THE LINALOOL-LIMONENE CONNECTION 

M.F. Leopold , William W. Epstein, and David M. Grant 

Department of Chemistry, University of Utah 

Salt Lake City, Utah 84112 

The advent of high-field NMR has allowed the accurate and reproducible 

measurement of relative deuterium intensities at natural abundance. Most recently 

this technique has been applied to the biosynthesis of limonene in citrus and 

the results supportlthe regiospeci~ic conversion of the proposed ~__-terpinyl 

cation to limonene. Study of the -H NMR of limonene suggested the analysis of 

an acyclic precursor such as linalool pyrophosphate. Both linalool acetate 

and limonene have been isolated from oil of bergamot and studied to assess 

continuity of relative deuterium integration and fractionation due to secondary 

deuterium isotope effects. 

.OPP 

I. Leopold, M.F.; Epstein, W.W.; Grant, D.M.J. Am. Chem. Soc. 1988, ii0, 616. 

140

A PROBE WITH HIGHER DECOUPLING EFFICIENCY AND 

F SENSITIVITY FOR SOLID STATE NMR EXPERIMENTS 

84 I 

Yi Jin Jiang * Warner R. Woolfenden Mark H. Sherwood Don W. Alderman 

Ronald d. Pugmire, and David M. Grant, Departments of Chemistry and Fuels 

Engineering, University of Utah, Salt Lake City, Utah 84112 

A more efficient double-tuned 13C/1H probe circuit has been developed espe- 

cially for higher decoupllng efficiency and improved sensitivity of the observa- 

tion channel (13C). 

Comparing this with the circuit in our previous paper (1), this modification 

of the circuit of the circuit not only eliminates an expensive capacitor, but 

also extends the space inside the probe, which lessens the arcing problem. 

Because the capacitor C4 has been replaced by a relatively small stray 

capacitance, the inductance L1 can be increased, resulting in a more efficient 

decoupling power in the sample coil. 

In a solid state NMR probe, for use at high frequencies (1H at 200 MHz or 

above) a small coil is often required, and hence the inductance of the coil is 

small. This decreases the sensitivity of the 13C channel. This problem can be 

alleviated by replacing the single X/4 coaxial cable in the original circuit (1) 

with three M4 cables in parallel, decreasing the inductance from ooint B to 

ground, and increasing the sensitivity of the sample coil of the 13C channel. 

(1) Yi Jin diang, Ronald d. Pugmire and David M. Grant, d. Magn. Reson. 71, 

485 (1987). 

COMPUTER PATTERN MATCHING IN 2D INADEQUATE SPECTRA 

85 I 

I 

Janet Curtis", Charles L. Mayne, Don W. Alderman, Ronald J. Pugmire ÷ and David M. Grant 

Department of Chemistry, University of Utah, Salt Lake City, Utah 84112 

+ Deparmaent of Fuels Engineering, University of Utah 

An automated system for extraction of 13C-13C connectivites as deteci~ by the phase-sensitive, 2D 

INADEQUATE NMR experiment is being developed. The cormectivites are contained in characteristic AX or AB 

patterns consisting of pairs of plus-minus doublets in the 2D data set which have equal double quantum 

frequencies, vl:X~. The software accepts a line list from a quantitative 1D 13C spectrum, sons the lines by intensity, 

and selects pairs with commensurate intensities to establish subsets of the full data set to be searched for a possible 

carbon-carbon bond. The program uses a simplex algorithm to perform non-linear surface-fitting for each coupled 

pair of spins. The adjustable parameters are intensities of the doublets, 1Jcc, the chemical shifts, and the T 2 

relaxation parameters. The double quantum frequency is simply the algebraic sum of the chemical shifts. For each 

statistically significant pattern obtained, a bond is assigned between the two coupled carbon nuclei. The antiphase 

doublets are a pattern more easily recognized in spectra with low S/N and the computer algorithm takes advantage 

of this additional information. 

The simulation routines will be described. The pattern matching software has been tested for spectra with up 

to 11 shifts and 10 couplings . . . . 

The objective of the research is the extraction of maximum information from the 2D INADEQUATE spectra 

in complex mixtures such as fossil fuels and in large natural product molecules, etc. 

141

86 THE USE OF J-SPECTRUM TYPE PULSE SEQUENCES 

IN COUPLED RELAXATION STUDIES 

Liu Fang*, Charles L. Mayne, David M. Grant 

Department Of Chemistry, University of Utah, Salt Lake City, Utah 84112 

The accuracy with which one can determine spectral densities in a coupled spin relaxation experiment is 

strongly dependent on the nature of the non-equilibrium states from which the spin system is allowed to relax. 

Pulse sequences similar to those used to obtain 2D J-spectra have been used to prepare initial non-equilibrium 

states of an AX2 spin system. Figure 1 shows partially relaxed 13C spectra from such a preparation. The sample 

studied was 1-decanol-l-13C. Table I compares the values of the relaxation parameters (spectral densities) and 

marginal standard deviations obtained from a dataset including the J-spectral preparation to those obtained from a 

dataset including only the preparations previously reported. Inclusion of data obtained using the new preparation 

significantly reduces the marginal standard deviations of several of the spectral densities and reduces correlations 

among the spectral densities. Thus, a significant improvement in the structural and dynamical parameters extracted 

from the spectral densities is achieved. 

V ----V---' 

Figure 1 

Table I: Spectral Densities for 1-Decanol-1-13C in Diglyme at 0 C. 

Spectral 

Density 

JAX 

JXX 

JXAX 

JAXX 

JA 

Jx 

i)o( 

Without J-Spectral 

Preparation 

0.09751 (0.00093) 

0.06625 (0.0068) 

0.00606 (0.0027) 

0.05794 (0.0013) 

0.0 (locked) 

0.05553 (0.0074) 

0.065 (0.0323) 

With J-Spectral 

Preparation 

0.09645 (0.00076) 

0.06219 (0.0033) 

0.00399 (0.0025) 

0.05635 (0.00091) 

0.0 (locked) 

0.06456 (0.0038) 

0.033 (0.0047) 

87 12D CHEMICAL SHIFT ANISOTROPY CORRELATION SPECTROSCOPY. A NEW 

SAMPLE POSITIORING MECHANISM WHICH SIMPLIFIES MEASUREMENT OF CHEMICAL SHIFT 

ANISOTROPIES IN COMPLEX SINGLE CRYSTALS. Mark H. Sherwood*, D.W. Alderman, & 

D.M. Grant, Dept. of Chemistry, University of Utah, Salt Lake City, UT 84112 

2D chemical shift anisotropy (CSA) correlation spectroscopy permits the 

measurement of CSA tensors in complex single crystals with far more peaks than 

have been tractable with 1D techniques (1). Such measurements open the 

possibility of using CSA tensors as structural and conformational probes in 

large molecules. The basis of the technique is to obtain 2D spectra in which 

the peaks are located by the chemical shift at two different single crystal 

orientations. The spectra are obtained by moving the crystal between the two 

orientations during the mixing time of a chemical exchange 2D pulse sequence. 

It will be shown how the complete CSA tensors for all the nuclei in a 

complex single crystal can be determined by measuring peak frequencies at only 

six well chosen orientations of the crystal and correlating these measurements 

with the 2D technique. The special geometry of a mechanism to accomplish the 

necessary orientation and reorientation will be explained and the device itself 

installed in a 200 MHz probe exhibited. In order to measure all the tensors in 

a single crystal the sample need be mounted only once in the mechanism and six 

2D spectra obtained. 

Six 2D spectra which determine the carbon-13 CSA tensors in a single 

crystal of sucrose will be shown. Sucrose has 12 carbons per molecule and two 

molecules per unit cell so that 24 peaks are observed. 

The possibilities of the technique for measurement of tensors in 

much more complicated molecules will be discussed. 

(1) C.M. Carter, D.W. Alderman, and D.M. Grant, J. Magn. Reson. 

6_55, 183 (1985) and 73, 114 (1987). 

142

88 I SOLID STATE ll3cd I~CLEAR }~GENETIC RESONANCE STUDY OF 

EXCHAI~GED ~.IOI~-~.IORII/X)NITES: Shelton Bank *a , Janet F. Bank a and 

Paul D. Ellis b Departments of Chemistry, aSUNY at Albany, Albany, 

New York 12222 and bthe University of South Carolina, Columbia, 

South Carolina 2920g 

The solid state ll3cd nuclear magnetic resonance spectra of 

cadmium adsorbed on montmorillonite clays were investigated. ~o 

cadmium oxoanion compents of different linewidths with different 

sensitivities to preparation conditions are identified. Echo train 

experiments at various temperatures indicate that the linewidths 

are governed by homogenous contributions rather than chemical shift 

dispersion. These results on cadmium environments are considered 

in relationship to models derived from adsorption studies of cadmium 

and other metals on clays and related materials. 

89 

13C NMR ASSIGNMENTS OF DNA OLIGONUCLEOTIDES AND THE DRUG NETROPSIN 

Eilis Boudreau, Tim Hyman, Steven LaPlante, Gilles Martin, Graham 

Jackson and Philip Borer. NIH Resource for NMR and Data Anaysis, 

Syracuse University, Syracuse, NY 13244-1200. 

13C nmr resonance assignments of DNA oligonucleotides have 

proceeded in two directions. The two-dimensional method is 

presented in a seperate poster by D. Cowburn and J. Ashcroft. The 

one-dimensional method uses spectral comparisons of chemical shift 

and chemical shift versus temperature:trends. We have applied a 

statistical analysis method, Bayes Maximum Likelihood, to the 

assignment of C-nmr spectra of the bases of oligonucleotides. 

We achieved 100% discrimination with the parameters chemical 

shift, temperature, a sequence factor representing the neighboring 

bases and the difference from the C5 carbon of the base. The 

technique produced 97% accuracy when used to characterize a 

spectrum previously assigned by the visual method. 

Netropsin is an anti-tumor,l~nti-cancer drug in which there is 

considerable interest. The C nmr resonances of the I d~g 

Netropsin have been assigned using the two-dimensional "H---C 

chemical shift correlated and the Attached Proton Test 

experiments. 

143

9o j 

THREE-DIMENS~ONAL STUCTURE DETERMINATION OF DNA: [d(TAGCGCTA) ]~. 

Sophia ~ang , Marc Delsuc +, George Levy, Philip Borer and Stev~n 

LaPlante , NMR and Data Processing Laboratory, NIH Resource and 

Biophysics Program, Syracuse University, Syracuse, NY13244-1200. 

+ICSN-CNRS 911 90, Gif-Sur-Yvette, France. 

The solution structure of [d(TAGCGCTA)] has been solved by 

NOESY-distance-restrained simulations. S~ructures determined by 

different methods were systematically compared (e.g. restrained 

dynamics and distance geometry analysis). Assignments have been 

completed for all the non-exchangeable proton resonances using NOESY 

and double quantum filtered COSY. NOESY spectra were acquired at 50, 

i00, 200, 400, 800 and 1200 msec. Volumes were obtained by several 

integration algorithms and those methods were compared. Completely 

isolated peaks and well resolved crosspeaks were used in the 

analysis. Distances were calculated from comparison of the initial 

NOE build-up rate with the reference distances (i.e. H2'-H2", H5-H6). 

I 91 OPTIMIZATION OF NMR DATAPROCESSING WITH PARALLEL 

COMPUTERS: Roy E. Hoffman* and George C. Levy, Northeast Parallel 

Architectures Center and NIH Resource, Bowne Hall, Syracuse 

University, Syracuse, NY 13244-1200, USA. 

For 40 years, most computers have been based on a single 

processor in what is known as the Von Neumann architecture. In 

the early 1970's, vector and array processors were introduced for 

scientific data processing and subsequently for NMR data 

reduction. It is only recently that computers with parallel 

processors have become widely available to NMR researchers and 

the advent of compilers with parallel and vector optimization 

has enabled the modification of algorithms in order to achieve 

speeds previously only possible with supercomputers. 

In this work an Alliant FX/80 system was used. This contains 

8 parallel processors, each with a vector facility, and has a 

maximum performance speed of 189 Mflops. With a physical memory 

of 128 Mbytes and a virtual memory of 2 Gbytes it is ideal for 2D 

and 3D-NMR processing. 

iD-Fourier transforms are 20 times faster on the Alliant 

than on a VAX 8800 and 120 times faster than on a VAX 11/750. 

However, the speed o~ a single processor on the Alliant when used 

without vector optimization is comparable to a VAX 8800. We 

report increases of computational speed for other algorithms such 

as 2D lineshape analysis, plotting, and peak-picking. These 

increases in speed are achieved in part by the optimization 

facilities in the compiler but much of the enhancement arises 

from changes in the source code. 

144

- - 92 l 

CHARACTERIZATION OF NORMAL BRAIN TISSUE USING MRI 

PARAMETERS AND A STATISTICAL ANALYSIS SYSTEM. Timothy J. Hyman*, 

George C. Levy, Department of Chemistry, Syracuse University, 

Syracuse, NY 13244, Robert J. Kurland, Jon D. Shoop, MRI Facility, 

Geisinger Medical Center, Danville PA, 17822. 

Doctors and scientis~ have been working toward techniques that 

utilize Magnetic Resonance Imaging for characterizing tissue types 

in the human body. Our study introduces a technique for the 

characterization of normal brain tissue. We will present a 

statistical analysissystem for discriminating 13 regions in the 

brain for 49 volunteers. The statistical method implemented in our 

technique is Bayes Maximum Likelihood which produced a 

discrimination accuracy of 90.8% for three sets of age groups. The 

method for calculating TI, T2 and proton density values implemented 

single-echo sequences, along with multiple-echo and inversion 

recovery sequences, in an effort to eliminate the affects of 

diffusion and of the inaccurate 90" pulse. T2 values calculated from 

single-echo images were found to have a higher accuracy of 

reproducibility and discrimination than T2 values calculated from 

multiple-echo images. The nine parameters showed excellent 

reproducibility with percent standard deviations between 7% and 18%. 

Finally, our study shows that a better discrimination is obtained 

when using all nine parameters rather than using just three 

traditional parameters or three averaged parameters. 

93 TOWARD A COMPUTER ASSISTED ANALYSIS OF NOESY SPECTRA: 

A MULTIVARIATE PATYERN RECOGNITION ANALYSIS OF 

DNA AND RNA NOESY SPECTRA 

Hans Grahn, Frank Delaglio, Ulf Edlundt, Mark W. Roggenbuck and Phil Borer* 


Syracuse University, NY 13244-1200. 

Two dimensional NMR spectra of biomolecules present us with a wealth of data. However, if we wish to 

access this information on a routine basis, automated methods for spectral assignment are essential, since 

the spectra are so complex. A 2D NOESY spectrum of a relatively small DNA or RNA fragment can contain 

several hundreds of cross-peaks. The situation is especially critical for RNA spectra, which typically include 

several regions of severe overlap or minimal resolution. Therefore, even the most basic task of selecting the 

peaks to be included in an initial analysis is difficult and time-consuming. For the same reasons, the actual 

procedures of manual assignment are also difficult. In this study we show that several of the above issues 

can be addressed by appealing to multivariate representations of the NOESY spectra. The analysis generates 

projections of the multivariate space by calculating principal components, with rather remarkable 

consequences. These projections directly identify relevant spectral bands. Subsequent multivariate analysis 

can provide peak assignment information according to type of base or conformation, and can even supply 

reliability estimates for proposed assignments, based on previously assigned spectra. The techniques are 

illustrated for separation of different structural segments of an RNA duplex NOESY spectra of 

(CACAUGUG) 2. 

NMR Research Group, Department of Chemistry, Ume~ University, S-901 87 Ume~, Sweden. 

14,5

94 

MULTIVARIATE TECHNIQUES FOR ENHANCEMENT 

OF TWO DIMENSIONAL NMR SPECTRA 

Hans Grahn, Frank Delaglio °, Mark W. Roggenbuck and George C. Levy 


Syracuse University, Syracuse 13244-1200. 

By using multivariate representations of 2D NMR spectra, we show that systematic noise 

such as tl and t2 ridges can be modeled by a Principal Component Analysis (PCA) method. 

Later these noise models can be subtracted from the original data without distorting the 

spectral features. 

In addition, PCA can generate reconstructions of 2D spectra, which are solely based on the 

systematic information from the data, and thus exclude random noise. Special data 

transformations can be applied in conjunction with PCA in order to emphasize or reduce 

specific features; this approach is employed in a diagonal suppression scheme for 2D NOE 

spectra. All of these methods can be combined to optimize data in preparation for 

automated, multivariate-based spectral analysis procedures, which benefit greatly from such 

improvements. 

- - NIH RESOURCE FOR MULTI-NUCLEI NMR AND DATA PROCESSING 

I AT SYRACUSE UNIVERSITY: Gregory J. Heffron*, Andrew 

95 ] S. Lipton, Karl D. Bishop, Steven R. Laplante, Philip 

N. Borer and George C. Levy, syracuse university, 

Bowne Hall, Syracuse, New York 13244-1200 

The NIH Resource at Syracuse University combines research and 

services in high sensitivity multi-nuclear nmr spectroscopy with 

advanced spectroscopic and other data processing capabilities. 

Emphasis is placed upon biological nmr and innovative processing 

methods. Instrumentation includes a General Electric GNS00 11.7 

Tesla multi-nuclear nmr spectrometer, a Bruker WM360 8.5 Tesla 

multi-nuclear nmr spectrometer, and a Cryomagnet Systems 5.8 Tesla 

multi-nuclear nmr spectrometer. Data processing facilities include 

five Sun-based SpecStations and a Stellar Graphics Supercomputer 

(May) networked with all of the spectrometers. Additionally, the 

Resource network is connected via Telnet and ftp to campus and 

worldwide networks, including several very powerful computers in 

S.U.'s Northeast Parallel Architectures Center. 

The "Syracuse concept" of nmr and computer networking will be 

presented with recent examples and tests of 2-dimensional maximum 

entropy Fourier spectral deconvolution processing on RNA and DNA 

data sets. These methods introduce few distortions and greatly 

clarify presentation of data. Users are welcome and inquiries may 

be directed to Gregory Heffron. 

146

96 

AN EVALUATION OF NEW PROCESSING PROTOCOLS FOR IN-VIVO NMR 

A.R. Mazzeo and G.C. Levy 

NIH Research Resource for Multi-Nuclei NMR and Data 

Processing, Syracuse University, Syracuse, NY 13244-1200. 

In-vivo NMR spectroscopy is often characterized by relatively 

broad resonances of low signal-to-noise superimposed on a 

curved baseline formed by broad but, in some cases, real 

resonances. A variety of processing techniques have been 

used in the past to obtain "quantitative" information from 

these difficult spectra, with varied success. Here, several 

different processing protocols, using software tools 

developed in this laboratory for spectral optimization, are 

used and evaluated for quantification of test spectra. Both 

synthetic and experimental data sets were processed using 

conventional techniques (convolution difference) and with new 

protocols involving Maximum Entropy Fourier Spectral 

Deconvolution (MEFSD) and Linear Prediction (LP). In some 

cases, baselines were corrected using an "intelligent" 

baseline conditioning routine. Results show the advantages 

and limitations of the various techniques. 

We would like to acknowledge NIH Grant RR-01317 for support. 

97 [2DNMR DETERMINATION OF '3C SPIN-LATTICE 

RELAXATION TIMES IN BPTI BY INDIRECT DETECTION: N.R.Nirmala~and 

Gerhard Wagner, Biophysics Research Division, University of Michigan, Ann 

Arbor, MI 48109. 

13C spin-lattice relaxation times provide an important clue for determining the 

mobility of a protein in solution. This is of interest in itself, but it is also essential for 

resolving ambiguities concerning variations in structures obtained from calculations of 

three-dimensional structures using NMR data. If there exists a high degree of mobility in 

only selected parts of the molecule, this will be reflected in the variation of spin-lattice 

relaxation times of the corresponding 13C nuclei. Therefore, knowledge of the 13C Tl's will 

aid in the study of three-dimensional structures of proteins in solution. Since typical 

spectra of proteins are heavily overlapped, individual 13C Tl's can be determined only by 

two-dimensional NMR. Furthermore, direct measurement of 13C spin-lattice relaxation 

times is hampered by the low sensitivity of the 13C nucleus, requiring long measuring 

times and high sample concentrations. Proton detection increases the sensitivity of the 

experiment by a factor of ( 7H/7c)2 and is therefore preferred. In the experiment 

described, a double transfer was used [1,2]. Proton magnetization was converted to 13C z- 

magnetization using a DEPT-type sequence. The 13C z-magnetization was then allowed to 

relax and reconverted to proton magnetization using a reverse DEPT sequence, with 

decoupling of the 13C nucleus during detection. The experiment was performed with 

natural abundance l aC on basic pancreatic trypsin inhibitor (BPTI). Individual Tl's of the 

u-carbons were determined. 

, 

1. L. E. Kay, T. L. Jue, B. Bangerter and P. C. Demou, J. Mag. Res., 73, 558 (1987). 

2. V. Sklenar, D. Torchia and A. Bax, J. Mag. Res., 73, 375 (1987). 

147

F 98 

I CHEMICAL EXCHANGE OF HETERONUCLEAR LONGITUDINAL 

TWO-SPIN ORDER (IzSz): A DYNAMIC PROBE OF CONFORMATIONAL 

ISOMERIZATION IN PROTEINS Gaetano T. Montelione* and Gerhard 

Wagner, Biophysics Research Division, University of Michigan, Ann 

Arbor, MI 48109. 

Chemical exchange spectroscopy can provide information about rates of 

conformational isomerization for systems which are in slow dynamic 

equilibrium. In such measurements it is often necessary to distinguish 

magnetization transfer through chemical exchange from cross-relaxation due 

to dipolar coupling. This distinction can be made by developing longitudinal 

two-spin order (i.e. zz-order) via scaler coupling within one conformer and 

transferring it by chemical exchange to the other conformer(s) which are in 

slow-exchange on the chemical shift timescale 1,2. We have employed this 

concept in developing 2D-NMR pulse sequences which characterize the chemical 

exchange of natural abundance heteronuclear two-spin order (IzSz). These 

"heteronuclear zz-exchange" experiments provide information about both rate 

and equilibrium constants for slow dynamic processes in polypeptides and 

proteins. The methods are applicable to studies of slow peptide-bond 

isomerization, aromatic ring rotations, and the folding / unfolding dynamic 

equilibria of small proteins. 

1. Bodenhausen et al. (1984) J. Mag. Reson. 59: 542. 

2. Wagner et al. (1985) J. Am Chem. Soc. 107: 6440. 

I -- 99 I TEACHING MRI USING COMPUTER ANIMATION, Joseph P. Hornak, 

Rochester Institute of Technology, l~ochester, NY 14623 

Involving undergraduate students in magnetic resonance research requires a carefully 

planned education program in the principles of magnetic resonance. Such a program often 

requires the student to learn the principles independently as there are usually no appropriate 

courses at the sophomore and jumor level. Several dynamic aspects of NMR spectroscopy and 

imaging are difficult for the student to understand when textbooks with static diagrams are used, 

and consequently, significant amounts of time are spent by the research advisor explaining these 

concepts which could better be taught by other means. One solution to this problem is to utilize 

computer animation for teaching magnetic resonance. A computer based teaching package of the 

basics of NMB. imaging is described which presents several of the dynamic processes of magnetic 

resonance with computer animation and text which simultaneously appear on a computer screen. 

Some of the topics taught by this package are the rotating frame, pulse sequences, the behavior of 

magr/etization during a two dimensional imaging sequence, and two dimensional Fourier 

transforms. 

148

. . 

I00 I NOVEL RESONATOR DESIGNS, E. Marshall, J.J. Listinsky, R.G. Bryant, 

J.P. Hornak, University of Rochester, Rochester, NY 14642 and Rochester Institute of 

Technology, Rochester, NY 14623 

Certain flat sample geometries and anatomies are not conveniently studied by NMR in a 

coil of cylindrical symmetry due to poor filling factor or on a surface coil due to signal roll-off. A 

single turn solenoid is a high efficiency transmit and receive coil with a nearly homogeneous RF 

magnetic field and sensitivity which may be used for NMR imaging and spectroscopy. We have 

designed a single turn solenoid with rectangular symmetry called a ribbonator. The LC circuit of 

the ribbonator is formed from a sheet of copper wrapped around a rectangular form. A gap 

between the two edges of the sheet is bridged by the capacitive elements of the resultant LC 

circuit. Ribbonators retain the favorable properties of a conventional cylindrical STS such as a 

high Q and nearly uniform excitation and receive fields. As a result the ribbonator efficiently 

produces MR signals from fiat objects placed within its volume. Holes may be cut in the side of 

the inductor to allow easier insertion of samples and do not significantly perturb its properties. 

The resonance equation for this rectangular parallelopiped shaped resonator will be discussed. 

Contour maps of the RF magnetic field along with images of the hand and wrist obtained from a 

ribbonator will be presented. 

101 

THE USE OF VARIABLE ANGLE SAMPLE SPINNING TO ASSESS AROMATIC CLUSTER 

SIZE IN COALS, COAL CHARS AND CARBONACEOUS MATERIALS 

Mark S. Solum °, Naresh K. Sethi, Julio C. FaceUi, Warner R. Woolfenden, 

Ronald J. Pugmire and David M. Grant 

Deparunents of Fuels Engineering and Chemistry, University of Utah, 

Salt Lake City, Utah 84112 

Variable angle sample spinning and powder pattern lineshape analysis techniques have been 

employed to study the 13C shielding tensov~ in bituminous coals, anthracites, inertinite macerals, and coal 

cha~. The shielding tensors have been analyzed as a superposition of different bands due to benzene- 

like, condensed (bridgehead and inner) and substituted carbons. A comparison of experimental data and 

theoretical calculations on model compounds containing 1-4 aromatic rings plus circumcoronene (C54HIs) 

support the interpretation of the shielding tensor data observed in coals and coal derived materials. 

Determination of the ratio of non-protonated to protonated aromatic carbons obtained on the coals, 

macerals, and chats by spectroscopic analysis are in good agreement with elemental analysis and previous 

dipoar dephasing NMR experiments. The method therefore constitutes a valuable way to analyze the 

strucnue of high rank coals and coal derived carbonaceous residues. The mole fraction of condensed 

inner ring carbons obtained by this technique is used to estimate the average cluster size in these 

polycondensed axomalic hydrocarbon materials. These data along with results from dipolar dephasing 

techniques on coals ate then used as input parameters in coal devolatization modeling. 

149

102 

] STRONG 181Ta OUADRUPOLE INTERACTIONS DETECTED VIA CROSS-RELAXATION 

TO HYDROGEN BY PROTON SPIN-LATTICE RELAXATION RATE STUDY IN TAB.322 : D.R. 

Torgeson*, J-W. Han and R.G. Barnes, Ames Laboratory + and Department of 

Physics, Iowa State University, Ames, Iowa 50011 

Proton spin-lattice relaxation rate R 1 measurements of hydrogen in the 

Ta2H metallic hydride phase of TaH 0 322 at 130 K have been made as a function 

of proton magnetic resonance frequencies from 24 to 105 MHz. Contributions to 

the proton Rl.arise from conduction elegl[ons, long-range diffusion (at higher 

temperatures) i an~ cross-relaxation by ISITa spins. 

The measured H relaxation rates R 1 show a strong, extremely broad (35 MHz 

wide) peak or collection R~ peaks centered at 70 MHz that we attribute to 

cross-relaxation by the 1°iTa spins which are themselves strongly relaxed by 

conduction electrons and quadrupole interactions. 

Interpretation of these resplls is complicated by the increasing strength 

of the Zeeman splitting of the ~SITa nuclear electric quadrupole energy levels 

that results from the stepped increase in the external magnetic field 

necessary for the proton R 1 measurements from 24 to 105 MHz. From these 

"spectra", we estimate the 181Ta pure quadrupole frequency ~0 to be - 40 MHz 

and the electric field gradient (EFG) asymmetry parameter-~-- 0.5. 

The orthorhombic crystal structure of Ta2H and the hydrogen occupation of 

alternate planes of tetrahedral interstitial sites within the structure 

indicate the crystalline EFG to have an asymmetry parameter ~ ~ 0.6. A more 

detailed interpretation of the results will be given, as well as a description 

of the experimental procedures employed to complete these measurements. 

+Operated for the USDOE by Iowa State Univ. under contract No. W-7405-Eng-82. 

1p.A. Hornung, A.D. Khan, D.R. Torgeson and R.G. Barnes, Z. Phys. Chemie Neue 

Folge 116, 577-86 (1979). 

i03 I PRE-PULSE SEQUENCE -- AN INVERSION PULSE (~) AND A 

DELAY TIME (aT3): . =Fu-Tyan Lin, Department of Chemistry, University of 

Pittsburgh, Pittsburgh, PA 15260 and Fu-Mel Lin, Calgon Corporation, 

Pittsburgh, PA 152~- 

The use of pre-pulse sequence which includes an inversion pulse 

(~) and a delay time (D 2) to null the intensity of a selected peak in 

NMR experiments was developed in this work. This delay time D 2 

defined as aT 3 is applied right after W pulse and before the pulse 

sequence for data acquisition. Here T 3 is a delay time to obtain 

zero magnetization for a sufficient long dealy time D 1 before ~ pulse. 

1 

T 3 is equal to (2n2)T 1 derived from Bloch equations, and =(I - ~)T 1 

measured from the experiments. For m~l~iple scans (n), the experi- 

(n-l)T3 z 

mental coefficient a = exp[- 4n(DI+A+I) ], where A is the free 

induction decay (FID) acquisition time. For a single scan with 

D 1 > 5T I, the a value becomes I. The presequence of inversion-delay 

has the advantages of selective suppression, more easier and accurate 

T 1 determination, and the separation of longer T 1 and shorter T 1 peaks 

of a molecule. 

150

104 

TAYLOR TRANSFORMATION OF 2D NMR "Um SERIES 

FROM TIME DIMENSION TO POLYNOMIAL DIMENSION 

FOR CONVENIENT DETERMINATION OF CROSS 

RELAXATION RATES IN NOESY SPECTRA 

Sven G. Hyberts* & Gerhard Wagner 

Biophysics Research Division, IST; University of Michigan; 

2200 Bonisteel Blvd; Ann Arbor, MI 48109 

A series of 14 NOESY specra with 1;m values ranging from 10 ms to 75 ms, was 

subject to a point-by-point Taylor transformation around l:m=0. This yields a 

zero-order spectrum containing the diagonal and base-line offset, a 1st-order 

spectrum containing only the cross relaxation rates and a 2nd-order spectrum 

containing the spin-diffusion and Tl-relaxation effects. To improve the signal- 

to-noise ratio we have truncated the Taylor expansion after the second order 

term. The cross relaxation rate can now be determined directly by integration of 

the desired cross-peak in the 1st-order spectrum. In the usual approach, the 

selected cross-peak has to be integrated in each 2D spectrum and then, the 

build-up curve has to be fitted to determine the cross relaxation rate. This is 

quite labour intensive for a macromolecule with many cross-peaks preventing 

the quantitative analysis of NOESY spectra in most structural work sofar. The 

method proposed provides a more convenient measurement of the cross 

relaxation Pates and may thus encourage quantitative analysis of NOESY 

spectra. 

- - lOS 

I 

EVALUATION OF DOUBLE TUNED CIRCUITS USED IN NMR: Toby Zens* 

Varian Associates, Palo Alto, CA 94303 

Double tuned circuits are frequently used in NMR probes as a 

simple means of exciting and detecting nuclei in a single coil 

device. General examples of different double tuned 

will be examined in terms of efficiency and 

application to NMR probes. Examples will include 

used in CPMAS and surface coil probes. 

151 

circuits 

practical 

circuits

1 0 6 I AR'nFACT'3 IN ECHO-PLANAR IMAGING 

Hector E. Avram * 1), Lawrence E. Crooks 2) and David M. Kramer 1) 

1) Diasonics MRI, 533 Cabot Rd., South San Francisco, CA 94080 

2) University of California, San Francisco, 400 Grandview Dr., South San Francisco, CA 94080 

Since its introduction in 1978 (1), Echo-Planar imaging has developed into a real clinical posibility for 

imaging of the human body when very high speed is required as in the case of uncooperative patients and 

children (2). Echo-Planar allows acquisition of an entire image in a time under 0.1 sec.. This technique is 

based on the use of succesive gradient-recalled echoes, individually phase encoded, to generate a 2DFT 

image. By switching readout gradient polarity, phase distortions occur which generate image artifacts 

mainly a ghost image L/2 away from the primary image (where L is the y-image dimension). It is found that 

these phase distortions which arise mainly from magnetic field inhomogeneities, gradient instabilities and 

eddy current distributions, are to a certain extent predictable and that with proper zero and first order 

phasing of the echoes such artifacts are minimized if not eliminated. 

A scheme for an efficient way to phase correct the phase encoded projections will be presented. 

(1) Mansfield P, Pykett IL, J Magn Reson 1978; 29:355-373 

(2) Crooks LE, et al, Radiology 1988;166:157-163 

... 107 

'I~VO DIMENSIONAL NMR SOFTWARE IN THE 

WORKSTATION ENVIRONMENT 

Frank Delaglio °, Pascale Sole1", Hans Grahnl", Alex Macur, 

John Begemann, Molly Crowther, Roy Hoffmanl", and George C. Levy. 

New Methods Research, Inc., 719 East Genesee Street, Syracuse, NY 13210. 

We present several techniques for optimal analysis of 2D NMR spectra, which rely both on the 

computational power and advanced graphics capabilities of modern scientific workstations. Examples 

include methods from the field of image processing, such as morphological filters, histogram 

equalizations, and various segmentation procedures. Such techniques, which improve data visibility, 

are most valuable when results can be obtained and examined quickly in an interactive scheme. 

Other examples involve surface fitting of 2D spectra, a task which is of course computationally 

strenuous, but also benefits from flexible graphics for presentation and evaluation of results. We use 

surface fitting to compensate for baseplane distortions, measure 2D NOE peak volumes, and to 

simulate DQF-COSY crosspeak multiplets. 

An outline of other methods newly implemented in the NMR2 two dimensional NMR software 

system is presented, including interactive bicomplex 2D phasing, 2D solvent signal subtraction, and 

connectivity analysis. We also illustrate our first-generation implementations for 3D NMR processing 

and presentation. 

"~ NMR and Data Processing Laboratory, NIH Resource and CASE Center, Syracuse University, 

Syracuse, NY 13244-1200. 

152

108 

PERFORMANCE COMPARISON OF DOUBLE-TUNED SURFACE COILS 

J.R. Fitzsimmons*, H.R. Brooker, W. Kuan, and B. Beck 

Departments of Radiology and Physics 

University of Florida, Sainesville, FL 32611 

Recently, several groups have tried to extend the utility of radio frequency (rf) 

coils used in NMR spectroscopy and imaging by designing rf coils which resonate at 

two or more frequencies (I-3). This study evaluates the advantages and disadvan- 

tages of several of the more recent designs suggested by the literature including 

one of our own making. In particular, we compare I) the design suggested by 

Schnall, et al (I) which makes use of rf "trap" circuits, 2) the loop gap resonator 

approach suggested by Grist, et al (2), 3) the transformer coupled planar design by 

Fitzsimmons, et al (3). In addition, a set of single tuned coils were constructed 

(85 MHz and 34 MHz) to serve as the standard for the above designs. All of these 

designs were constructed using the same conductor type (#14 solid copper), capacitor 

type (Sprague IOTCC series), diameter coil (4.8cm) and balanced matching scheme. 

Two phantoms were used for these experiments, one containing DeO and saline to 

approximate the loading effects of the human arm muscle and the other using dilute 

phosphoric acid with saline. The unloaded and loaded Q of each coil was measured 

using a sweep generator and 50 ohm bridge and each coil was evaluated on a 2.0T SIS 

imager/spectrometer using a one pulse experiment. Signal to noise (S/N) measure- 

ments were made for each coil at each frequency. Significant differences were found 

between coils and within coils on different frequencies. 

This research is supported by grants from the National Institute of Health 

(P41-RR-02278) and the Veterans Administration Medical Service 

I. Schnall, MD, Subramanian, VH, Leigh, JS, and Chance, B. J. Magn. Resort. 65, 

122-129 (1985). 

2. Grist, T.M., J.B. Kneeland, A. Jesmanowicz, W. Froncisz, and J.S. Hyde. 

Fifth Annual Meeting of the Society of Mag. Res. in Med. August, 1986. 

~. J.R. Fitzsimmons, H.R. Brooker, B. Beck, Mag. Res. In Med. 5,471-477,1987. 

I-- 10g I NMR STUDY OF ALKALINE HYDROLYSIS OF POLY-(ACRYLONITRILE) 

(PAN): J. Lovy*, V. Stoy, Kingston Technologies, Inc., Dayton, New 

Jersey, 08810. 

Although alkaline hydrolysis of PAN has been utilized commercially 

as well as studied for many decades, its mechanism was not sufficiently 

known. 

According to the former studies, the mechanism of hydrolysis of 

PAN was essentially identical with hydrolysis of an isolated nitrile 

group. The formation of cyclic groups of tetrahydronaphthyridine type 

was suggested as a mere minor by-product. 

By detailed NMR study we have found that products of alkaline 

hydrolysis contain acrylamidine (which was never reported before) in 

substantial concentrations. Its formation requires a cyclic mechanism 

involving at least two CN groups in 1,3 position. 

The further studies of akaline hydrolysis of PAN and a model 

compound (glutaronitrile) have shown that the cyclic mechanism is the 

dominant one. The influence of reaction conditions and media was also 

studied. 

153

1 1 0 

-- [ DISCRETE ANALYSIS OF STOCHASTIC NMR USING WIENER SERIES: 

S.T.S. Wong*, R.D. Newmark & M.S. Roos, Donner Laboratory, Lawrence Berkeley Laboratory, University 

of California, Berkeley, California 94720. 

Stochastic NMR is an efficient alternative to conventional NMR techniques for spectroscopy and imaging 

that can reduce the peak RF power requirement by several orders of magnitude. The stochastic experiment 

is analysed by a Wiener series expansion of the non-linear NMR system with a discrete Gaussian white noise 

process for the input. This diifers from Kaiser's analysis for continuous excitation (JMR 48, 293, 1982). A 

method for correcting the distortions in spectra (images) reconstructed by simple 1D cross-correlation due to 

the NMR system non-linearity will be presented. 

The experiment consists of a series of RF pulses with Rip angles being a sample of a discrete Gaussian 

white noise process. One data point is sampled after every RF pulse. Spectral (image) information is obtained 

by Fourier transforming the 1D cross-correlation of the sampled data points with the white noise sequence. 

By modeling the system with a set of difference equations, analytic expressions for the signal power and 

the reconstructed spectra (projections) were obtained. These expressions allow us to choose the Rip angle 

variance which maximizes signal-to-noise ratio. Unfortunately, the Rip angle variance that gives the maximum 

signal-to-noise ratio is large enough to cause the magnetization response to saturate, giving rise to distortions 

in the reconstructed spectra (projections). 

When the non-linear magnetization response is expanded into a Volterra series, the desired non-distorted 

spectrum corresponds to the linear kernel, hl, of the series. However, there is no easy way to obtain hl 

theoretically or experimentally. The non-linear response cam be expanded into a series of Wiener functionals 

which can be obtained by multi-dimensional cross-correlations of the sampled data with the Gaussian white 

noise excitation. The 1D cross-correlation gives the first order Wiener kernel, kl, which approaches hl as 

the Rip angle variance approaches zero. As the system becomes more non-linear, hl becomes dispersed into 

Wiener functionals of order higher than one: hl = kl + ki(3) + k1(s) + ...... , where k](3), k1(s) etc., are the linear 

components of the higher order Wiener functionals. Expressions for kl, ki(3) and k1(s) have been derived. 

The sum/=i + ki(3) reduces the distortions significantly for the Rip angle variance which gives the maximum 

signal-to-noise ratio. 

11 1 J STOCHASTIC NMR IMAGING WITH OSCILLATING GRADIENTS: 

S.T.S. Wong, M.S. Roos*, R.D. Newmark, Donner Laboratory, Lawrence Berkeley Laboratory, University of 

California, Berkeley, California 94720. 

The analysis of NMR imaging and volume selective spectroscopy with oscillating gradients (A. Macovski, 

J. Mag. Res. Med., vol. 2, p. 29-39, 1985) has been extended to include stochastic excitation. Advantages of 

the method described relative to conventional techniques are a large reduction in the peak RF power required 

relative to deterministic pulse excitation and the elimination of switching transients using oscillating gradients. 

The stochastic experiment consists of a sequence of RF pulses where the Rip angles are a sample of a 

discrete Gaussian white noise process. One data point is sampled after every RF pulse in the presence of a B0 

gradient which varies sinusoidally throughout the experiment. The magnetization response to RF excitations 

is assumed to be linear, which is valid in the limit of small Rip angles. The sampled signal is then cross- 

correlated with the product of the Gaussian white noise sequence and a phase demodulation kernel derived 

from the time-varying gradient waveform in order to reconstruct an image. 

The expected value of the reconstructed image has the form of a localization function convolved with the 

spin distribution. This function is 

e -°/T' 3o (2~Gsin(WmO'/2) z~, 

\ Wm / 

where 3o is the zero-order Bessel function, G and co. are, respectively, the amplitude and frequency of the 

siausoidal gradient. The time lag of the cross-correlation, o, is a free parameter that may be used to manipulate 

T2 contrast. Integrating over o also improves localization, resulting in Jo(TGz/a~,n). The sidelobes of the 

localization function can be reduced by including harmonics of the gradient frequency in the kernel, allowing 

synthesis of a localization function from a series of Bessel functions of increasing order. 

The variance of a given pixel of the image obtained by cross-correlation does not approach zero in the 

limit of infLnite observation time. It becomes part of the overall image noise in additon to observation noise. 

Both types of noise can be reduced by averaging images reconstructed using separate samples of the excitation 

process. 

154 

. - -

RECENT EXTENSIONS OF NOESYSIM, A PROGRAM FOR RAPID COMPUTATION 

112 [OF NOESY INTENSITY MATRICES FROM ATOMIC COORDINATES AND EXPERI- 

MENTAL CONDITIONS. Hugh L. Eaton*, Niels H. Andersen, and Xiaonian Lai, University of Wash- 

ington, Seattle, WA 98195. 

The NOESYSIM program has been extended to allow calculation of NOESY matrices at any of 

four levels of theory or approximation: 1) linear-limit isolated spin pairs; 2) isolated spin pairs with 

leakage correction; 3) summation over all possible three spin systems; and 4) complete experiment 

simulation by numeric integration (J. Magn. Reson. 74, 212). The latter implicitly includes 

all spins and is equivalent to CORMA (Borgias and James, 28th ENC) for idealized experiments 

with an effectively infinite repetition interval. Methods 3) and 4), which yield matrices that lack 

diagonal symmetry for experiments with short repetition times, give superior agreement with 

experimental data. We find that the three spin approximation, which requires considerably less 

computation time than method 4, holds to 4- 10% for all systems examined throughout the range 

wr c = 0.18 - 12. The three spin approximation thus appears to be suitable for conformational 

refinement procedures based on experimental NOESY data. In contrast, we find that isolated spin 

pair approximation frequently yields NOESY cross-peak intensities that differ from exact theory by 

as much as a factor of 3, which corresponds.to as much as a 40% error in distance estimates. 

For the purposes of NOESY analysis carried-out without computer assistance, the three spin 

approximation is equivalent to 

1 {S~j Sj~ rm 

27" m k Sii "}" Sj3 } = Oi~ "}- -2- Z tTjk Oki 

k 

an equation that holds to better than 10% throughout the correlation time range that is found for 

molecules in solution states amenable to high resolution NMR. 

[-- 

{ 115 [alp MAGNETIC RESONANCE IMAGING OF SOLID CALCIUM PHOSPHATES: 

POTENTIAL FOR CHEMICAL IMAGING OF BONE: Jerome L. Ackerman, a Daniel P. Raleigh, *b,c and 

Melvin J. Glimcher; a aDepartment of Radiology, NMR Facility, Massachusetts General Hospital Boston, MA 

02114; bDepartment of Chemistry, Massachusetts Institute of Technology Cambridge, MA 02139; CFrancis Bit- 

ter National Magnet Laboratory, Massachusetts Institute of Technology Cambridge, MA 02139; aLaboratory 

for the Study of Skeletal Disorders and Rehabilitation, Department of Orthopedic Surgery, Harvard Medical 

School, Children's Hospital Medical Center, Boston, MA 02115 

The use of NMR imaging of biological systems has been almost exclusively restricted to the fluid com- 

ponents of tissues. An exciting possible application of NMR imaging is that of imaging of the phosphate 

resonance in mineralized tissue. Previous spectroscopic experiments have demonstrated the potential of 31p 

NMR in elucidating the chemical composition of the mineral phase of bone. With the eventual goal of ex- 

tending these measurements to the imaging domain, we have been developing methods for the production of 

phosphorus images in calcium hydroxyapatite (an accepted model for the major mineral phase of bone). 

We have obtained one-dimensional projections of the alp resonance in synthetic hydroxyapatite for speci- 

mens oil the order of 0.5 to 1.0 cm in linear extent at 7.4 T field strength. Because of the solid state nature of 

these samples, short alp spin-spin relaxation times under 1 msec occur, necessitating echo times on the order: 

of 1 msec and phase-encoding magnetic field gradient pulses under 500 /zsec. Although such T3 values are 

easily managed by spectrometers, they are well below the range of minimum echo times (typically 15 msec or 

greater) achievable by clinical imagers. Optimal projection quality and shortest total image acquisition times 

result from pulsed gradient phase-encoding of the spatial dimension, using a compensating gradient pulse to 

cancel the distorting effects of gradient waveform transients. The exceedingly long alp spin-lattice relaxation 

times could lead to potentially intolerable image acquisition times; we have reduced these with a flipback 

pulse teclmique. These methods should be of general utility in the multinuclear imaging of a wide variety of 

solids of interest in biophysics .and the materials sciences. 

155

-- VOLUME LOCALIZED SPECTRAL EDITING USING ZERO 

QUANTUM COHERENCE CREATED IN A STIMULATED ECHO 

1 1 4 [ PUI~E SEQUENCE: Christopher H. Sotak and Dominique M. Free- 

man, General Electric NMR Instruments, Fremont, CA, 94539. 

With the advent of myriad pulsed field gradient methods for volume localization, it is now 

possible to obtain reasonable in vivo specua from a region of interest based upon an image. For 

protons, we have found the STimulated Echo (STE) technique (1-4) to give good results. Unfor- 

tunately, the direct observation protonated metabolites /n vivo is frequendy precluded by the pres- 

ence of interfering resonances. Consequently, some method of spectral editing is usually required, 

in conjunction with the localization technique, to extract the metabolite information. 

We have developed a volume localized spectral editing technique using zero quantum 

coherences (ZQC's) created in a STE pulse sequence (5). In addition to localization, the STE 

sequence (Figu£roe 1) generates ZQ (and higher order) coherences in coupled spin systems following 

the first two 90 pulses. The ZQC's evolve during the interval t 1 and manifest themselves as an 

amplitude modulation of the corresponding single quantum sign~tl generated following the third 

90 pulse. The ZQ modulation frequency equals the chemical shift difference (in Hz) between the 

coupled spins. Noncoupled spins, on the other hand, experience no modulation during the t 1 

period since isolated spin-lf2 nuclei only undergo single quantum transitions. Subtracting two 

volume localized spectra with the appropriate ZQ evolution periods constructively adds signal 

from metabolites with coupled spins and cancels signal from interfering noncoupled resonances. 

In addition to discriminating against noncoupled spins, it is also possible to distinguish 

among various types of coupled spin systems based upon differences in their ZQ frequencies. 

These frequencies are elucidated in a two-dimensional experiment where the ZQ evolution period 

is incremented. Subsequent two-dimensional Fourier transformation yields a plot of chemical shift 

vs. ZQ modulation frequency. Peaks due to coupled metabolites are separated in the ZQ fre- 

quency domain based upon chemical shift differences between the respective coupled spins. Peaks 

due to noncoupled spins appear at zero frequency. 

We have applied these techniques /n vivo to measure 5 to 10 mM lactate concentrations in 

implanted mouse tumors in the presence of interfering lipid resonances. 

1. J. Frahm, K. D. Merboldt, and W. Hanicke, J. Magn. Reson. 72, 502 (1987). 

2. G. McKinnon, Works in Progress, 5th Annual Meeting of the Society of Magnetic Resonance 

in Medicine, Montreal, August 19-22, 1986, 168. 

3. J. Granot, J. Magn. Reson. 70, 488 (1986). 

4. R. Kimmieh and D. Hoepfel, J. Magn. Reson. 72, 379 (1987). 

5. C.H. Sotak and D. M. Freeman, J. Magn. Reson., in press, (1988). 

C 

O 

I C 

115 

I [ USE OF PURE ABSORPTION PHASE 31p/IH 2D COLOC 

NMR SPECTRA FOR ASSIGNMENT OF zip SIGNALS OF OLIGONUCLEOTIDES: 

Josepha M. Fu, Stephen A. Schroeder, Claude R. Jones*, Robert Santini* and David G. Goren- 

stein*, Department of Chemistry, Purdue University, W. Lafayette, IN 47907 

Chemical shift data in 31p NMR spectroscopy serves as an important probe of the conformation 

and dynamics of nucleic acids. A major limitation in the use of zip NMR has been the difficuly 

in assigning the signals. An 1tO labeling methodology has previously been used for assigning 

the zip signals, however, this methodology is rather costly and time consuming. A 2D 31p _ 

1H COLOC NMR approach is shown to provide a staightforward, convenient alternative for 

assigning the zip of even moderately sized oligonucleotide duplexes. The COLOC pulse sequence 

was modified to emphasize 31p _ 1H scalar couplings and to produce pure absorption ph~qe 

spectra. The 31p _ l H COLOC spectra showed enhanced sensitivity and resolution relative to 31p 

- 1H heteronuclear correlation spectra. The 31p chemical shifts of the self-complementary 14 base 

pair oligonucleotide, d(TGTGAGCGCTCACA)2, were determined from the COLOC spectrum, 

based upon IH assignments determined by 2D 1H - tH COSY and NOESY spectra. The zip 

assignments were verified by 1~O labeling. The zip chemical shifts of another oligonucleotide, 

d(TATGAGCGCTCATA)2, were also determined by 31p _ l H COLOC and 1H - IH COSY and 

NOESY. 

156 

C 

N 

k

116 ] 

NODIFICATIONS TO A JEOL GX270 WIDEBORE SPECTROMEI'ER 

FOR NAGNETIC RESONANCE IMAGING: PETROGRAPHIC APPLICATIONS 

By 

National 

Daryl A. Doughty and Nicida L. Maerefat 

Institute for Petroleum and Energy Production 

Bartlesvllle, OK 74005 

ABSTRACT 

Modification of an existing jEOL GX270/89 NMR spectrometer for imaging 

studies is described. Inhouse modifications were made because of the 

specialized nature of the petrographic samples and their restrictions on probe 

geometry. Because of the wide proton linewidths measured at 270 MHz for 

fluids contained in porous rock the magnetic field of the spectrometer was 

reduced to 1.41T (60 MHz proton frequency) for the imaging studies. Details 

concerning the probe/gradlent coil assembly and the spectrometer interface 

board containing the gradient control and slice-selection circuits are 

presented. Results showing the operation of the spectrometer in imaging 

phantoms, brine in sandpacks, and fluids in Berea, Cottage Grove, and 

Cleveland sandstone cores are also presented. 

11 7 J RESONANT EFFECTS IN CP-MAS SPECTRA OF HOMONUCLEAR 

DIPOLAR-COUPLED SPIN SYSTEMS ~ Thomas M. Barbara and Gerard S. Harbison: 

Department of Chemistry, SUNY at Stony Brook, Stony Brook, NY 11794-5400 

The CP-MAS spectra of systems which contain homonuclear dipolar couplings between inequivalent spin-I/2 

sped,,, exhibit sisnlflcant broadening of the coupled resonances, which is particularly pronounced when the rotational 

frequency vr is • areal/integer multiple of the isotropic chemical 8hilt difference between the nuclei ~6. This resonant 

effect has been known for over 20 years but has recently attracted considerable interest. We have developed two 

formalissm for underetendlng and calculating the lineshspes of these systems. The first involves a basis transformation 

to • rotating frame which reduces the problem to the fsmJ/Jar double-resonance ¢~e for • two-level system. In the 

simplest pmudble model system which exhibits these phenomena (two coupled spin= without • ahlelding anlsotropy 

but with distinct isotropic chemical shifts) the solution of the equations of motion for the on-resonance case, where 

A6 -- J0r or 2~'r, gives • splitting which is linearly proportional to the dipolar coupling and dependent on the angle 

p between the dipolar and the rotor axis. This anKsdar-dependent splitting leads in unoriented samples to scaled 

powder patterns, whose quite distinct shapes for A6 ----- JPr and A6 = 2vr reflect the different dependence on/~ of 

these two rotor resonances. The width of these patterns is simply (~/'2D/'.~) 6n~l DI~ for Che ~, ~.d ;;r r=o-=ce~ 

respectively, (D being the dipolar coupling). These values, while exact only for vonishin~y small D, are correct 

to within S% for D < =*r- Dipolar effects when A6 ~ =*r or 2=*r can similarly be viewed as Bloch-Siegert shifts 

Jn the double rwommce formalism. These shifts are asaln an83dar-dependent and therefore also lead to apparent 

line-broadening; they also causo the center of the sis~al to be ahifted away from its uncoupled frequency. 

Chemical shielding anleotropy destroys these sim~le relationships between the linewidth and dipolar coupling; 

it also causes resonances to appear at nvr for n y~ I or 2. The double-resonance picture is however still intuitively 

useful, and gives magnitudes for the dipolar linewidth, particularly off-resonance. To calculate exact lineshapes in 

these cases, we have used • numerical solution to the Liouville equation mdng a Rnnge-Kutta algorithnL This is 

surprisingly modest in its use of computer time, and can be used to calculate spectra to • high degree of accuracy. 

Spectra c~Iculsted ~ this method are in excellent alpreement with experimental results ond with those of the double 

resommce fonnalim~ The advantages of the method are that it does not require assumptions about the ¢yc]Jcity of 

the interactien= (as average Hami]tonlen theory does), their relative aises or the sdiabaticity of the perturbations, 

and that it can be extended with little modification to almost any theoretical problem in NM~ 

157

118 l APPLICATION OF N-H HETERONUCLEAR CORRELATION 

SPECTROSCOPY TO SEVERAL 15N ENRICHED PROTEINS 

Ed S. Mooberry* , Brian J. Stockman, Bin Yuan, Byung Ha Oh, and John L. Markley 

National Magnetic Resonance Facility at Madison and Department of Biochemistry, 

College of Agricultural and Life Sciences, University of Wisconsln-Madlson, Madison, 

WI 53706 

Several applications of N-H heteronuclear correlation spectroscopy (HETCOR) are 

described for 15N enriched proteins. An experimental arrangement is shown for 

obtaining 15N decoupled spectra. The proton chemical shift is removed from the 

nitrogen dimension by using time proportional phase incrementation. Examples are 

shown for [95% ul 15N]Anabaena 7120 flavodoxin (I), [95X ul 15N]Anabaena 7120 

ferredoxln and [95% 15N-Leu]staphylococcal nuclease . The HETCOR spectra were 

obtained by using Bruker reverse electronics with the new 451MHz IF frequency and a 

5--- reverse probe. Water elimination was accomplished by solvent presaturatlon for 

the flavodoxin and ferredoxin spectra. For nuclease, the spln-echo sequence (without 

decoupling) recently published by Sklenar and Bax was used (2). 

I. B.J. Stockman, W.M. Westler, E.S. Mooberry, and J.L. Markley, Biochemlstry'27, 136- 

142 (1988). 1 

2. V. Sklenar and A. Bax, J. Magn. Res. 74, 469-479 (1987). 

[Supported by NIH Grants RR02301, RR02781, and GM35976, NSF Grant PCM-845048, and 

USDA Competitive Research Grant 85-CRCR-I-1598.] 

119 I 13C LABELING AND HIGH RESOLUTION 1H 2-D NMR: MAKING 

UNNATURAL ESTERS STAND UP AND BE COUNTED 

G.L. Helms~ W.P. Niemczura and R.E. Moore; Dept. of Chemistry, 

University of Hawaii, Honolulu, HI. 96822 

Polyhydroxylated natural products which also contain ester func- 

tionalities can be formidable structure problems. It is often 

necessary to peracetylate these compounds to alleviate solubility 

problems or to increase spectral dispersion. Unfortunately the 

sites of natural esterification now become indistinguishable from 

those of the introduced esters. Ace~ylg~io ~ with 1,1'-'~C acetic 

anhydride yields products in which -J --C--H couplings label the 

sites of the introduced esters. These small couplings (I-4 Hz) 

can be visualized even in crowded spectral regions by using 

homonuclear H 2-D J Resolved or high resolution phase sensitive 

COSY spectra. In both cases the heteronuclear coupling leads to a 

splitting of the cross peak multiplet patterns in the F2 dim- 

ension. This splitting not only indicates the location of t~e 

introduced esters but also allows the determination of the-J 

heteronuclear coupling constant. Examples taken from our work on 

novel cyclic peptides and cyclodextrins will be presented. 

158

I 

12 o I SPECIATION OF WATER IN GLASSES BY HIGH-SPEED 1H MAS-NMR 

Hellmut Eckert *+, James P. Yesinowski*§, Lynn A. Silver Y , and Edward M. 

Stolper ¥, + Department of Chemistry, UC Santa Barbara, Goleta CA 93106, 

§Division of Chemistry and Chemical Engineering, California Institute of 

Technology, Pasadena, CA 91125, YDivision of Geological and Planetary 

Sciences, California Institute of Technology, Pasadena, CA 91125. 

The state of water in silicate glasses has received considerable attention both 

in geology and materials science and much effort has been devoted to 

identifying and quantitating the H20 and OH species present. This work 

describes the first application of high resolution 1H nuclear magnetic resonance 

methods to this problem. 1H MAS-NMR results are reported on a series of 

synthetic and naturally-occurring silicate glasses containing 0.04 to 9.4 wt.% 

H20. Spinning at 8 kHz results in substantial line-narrowing; in addition, 

extensive spinning sideband patterns are observed that reflect the 

inhomogeneous character of the 1H-1H dipolar couplings within anisotropically 

constrained water molecules. The 1H MAS-NMR spectra can be simulated as the 

sum of the individual spectra of the model compounds tremolite (OH) and 

analcite (H20), and the species concentrations thus obtained are in good 

agreement with IR results. The agreement of the experimental 1H MAS-NMR 

spectra with simulations based on compounds, in which the hydrogen-bearing 

species are structurally isolated, indicates that no preferential clustering 

occurs. 

121 J BROADBAND SPIN DECOUPLING IN THE PRESENCE OF SCALAR INTERACTIONS 

A. J. Shaka ~, C. J. Lee and A. Pines, University of California, Berkeley, 

Berkeley, California 94720 

Successful broadband spin decoupling sequences like WALTZ-16 are based on 

an underlying model of isolated IS spin pairs. Almost all organic molecules 

of interest, however, contain networks of scalar-coupled protons. We have 

analyzed the effect of proton scalar coupling on broadband decoupling and 

devised a new series of broadband decoupling sequences which we call the 

DIPSI sequences. The DIPSI sequences of'fer the same high standard of decoupling 

as WALTZ-16 in the isolated IS case, but over somewhat smaller bandwidths. 

in the presence of proton-proton coupling the DIPSI sequences are superior 

to WALTZ-16, offering an improvement in resolution and sensitivity for 

carbon-13 spectroscopy. 

The principles used to construct the DIPSI ~eq,,~nrP~ can be applied to 

a number of related experiments in two-dimensional spectroscopy. 

159

1 22 I IMULTINUCLEAR TWO-DIMENSIONAL APPROACHES TO SEQUENCE-SPECIFIC 

RESONANCE ASSIGNMENTS IN A PROTEIN: 13C-13C, 13C-15N, IH-13C, IH-15N, AND IH-IH 

CORRELATIONS IN ANABAENA 7120 FLAVODOXIN: Brian J. Stockman*, William M. Westler, Ed 

S. Mooberry, and John L. Markley. Department of Biochemistry, College of Agricultural 

and Life Sciences, 420 Henry Mall, University of Wisconsln-Madlson, Madison, WI 53706. 

A sequential assignment procedure based on heteronuclear correlations is presented. A 

two-dlmensional (2D) 13C[13C] Double Quantum Correlation (DQC) NMR experiment (125.76 

MHz) has been applied to [26% ul 13C]flavodoxin (MW 21,000). The uniqueness of the 

carbon spin systems for 18 of the 20 amino acid types (Asx and Glx degeneracies can be 

distinguished via 13C-15N correlations) allowed many aliphatic and aromatic side 

chains to be completely outlined, ending with the carbonyl carbon. Carbon spin 

systems were then sequentially assigned in the following way. Carbonyl assignments 

were extended across the peptide bond to the alpha nitrogen of the following residue 

using 2D 13C-15N correlations of [26% ul 13C, 95% ul 15N]flavodoxin. Amide protons 

were assigned using 2D IH-15N correlations (H20 solvent), and were correlated to the 

alpha carbon protons of the same residue by a double-quantum-filtered COSY experiment. 

2D IH-13C correlations were then used to cross assign alpha protons to alpha carbons, 

thus allowing identification of the following residue via its carbon spin system. 

Alternatively, 13C-15N correlations could be used to assign the alpha carbons of the 

next residue (both procedures could be used for redundancy or to overcome unfavorable 

resolution). The advantages of using this strategy for sequential assignments 

compared to a homonuclear iH-IH strategy are the relative ease with which carbon spin 

systems can be assigned in comparison to proton spin systems, and the reliability of 

correlations based on scalar coupling as opposed to dipolar coupling. Assignments can 

be extended to side-chain proton spin systems via IH-Ioc correlations to carbon spin 

systems. [Supported by USDA Competitive Research Grant 85-CRCR-I-1589, NSF Grant 

RR023021, and NIH Grants RR023021, RR02781, and GM07215.] 

SOLID STATE NUCLEAR MAGNETIC RESONANCE INVESTIGATIONS OF 

123 I ORGANOPHOSPHONIC ACID ADSORPTION ON ALUMINA 

Neal R. Dando; Larry F. Weiserman and Edward S. Martin 

Aluminum Company of America, Alcoa Technical Center, Alcoa Center, PA 15069 

Methyl and phenyl phosphonic acid adsorption on gan~na alumina was investigated by 

phosphorus-31, carbon-13, and aluminum-27 solid state NMR spectrometry. The 

population of chemisorbed and physisorbed species was investigated over a 5-20% 

loading range. Physisorption was observed at the lowest loading studied (5%) and 

increased monotonically as a function of loading. The population of chemisorbed 

species remained constant throughout the loading range studied. Motional dynamics 

of the adsorbed species were evaluated by a series of static, magic angle spinning, 

high power decoupling and relaxation experiments. Carbon-13 and aluminum-27 data, 

while less sensitive to surface phenomena, allowed for more complete characterization 

of the substrate and adsorbates. 

1 6 0 - - -

124 

I A COMPLETELY INTEGRATED NETWORK OF HOME--BUILT 

AND COMMERCIAL NMR SPECTROMETERS. Donald A. Bouchard* 

and Stanley J. Opella, Department of Chemistry, Univ. of Pennsylvania, 

Philadelphia, PA 19104-6323 

A description of a local-area laboratory network consisting of three home- 

built DEC microVAX-II controlled spectrometer nodes, two DEC PDP- 

11/23 commercial spectrometer nodes, and a central data-processing node 

will be presented. The design of the microVAX-II home--built spectrometers 

will also be presented. The spectrometer software provides a system to de- 

sign and execute NMR experiments of any complexity, integrating the large 

base of existing applications with NMR spectroscopy. The local-area NMR 

network is bridged to a departmental computer facility consisting of a VAX 

11/785 and 1i/750 each utilizing DECnet and TCP/IP networking protocols, 

providing transparent links to most national and international networks. 

125 NMR vs. CIRCULAR DICHROISM: WrHAT CAN WE SAY ABOUT 

HELICITY? Ronald W. Behling,* Peter A. Mirau, and Lynn W. Jelinski, AT&T Bell Laboratories, 

Murray Hill, NJ 07974. 

The S-peptide is formed by enzymatic cleavage of ribonuclease A, and is composed of amino acids 1 - 

20. The S-peptide can be recombined with residues 21 - 124 (the S-protein), and this non-covalent 

complex is enzymatically active and its crystal su'ucture is known. The crystal structure shows that 

residues 3 - 13 form an a-helix that is virtually identical to the (x-helix formed by residues 3 - 13 in 

intact ribonuclease A. Circular dichroism studies suggest that the S-peptide is approximately 50% 

helical under certain salt, pH, and temperature conditions. 

We present results that address the question: what does 50% helical mean? High resolution proton 

NMR spectra were obtained for the S-peptide in 1.0 M NaC1, pD 5.3, and 0 *C. These spectra include 

2D-double quantum filtered COSY, 2D-NOE, and selective and non-selective T: experiments. The 

relaxation experiments suggest that the S-peptide in solution has dimensions that are substantially 

different from those predicted from the crystal structure, and that considerable internal motions are 

present. The measured 2D-NOE was compared with the 2D-NOE calculated from the crystal structure. 

The experimental NOE's are substantially different from the predicted NOE's, illustrating that all of the 

details of the peptide conformation are not preserved in solution. 

161

126 I 

EXPERIMENTAL EVALUATION OF NMR IMAGING PROBES 

S. L. Talagala* and L. D. Hall, Department of Chemistry, 

University of British Columbia, Vancouver, B.C., Canada 

Several probe designs suitable for high field NMR Imaging have been 

suggested in the recent years to overcome the deficiencies of traditional 

solenoid and saddle shaped coils. The variety of designs proposed demonstrate 

the difficulty in optimizing all necessary criteria with a single design. 

This study presents an experimental evaluation of the performance of four 

commonly used probe designs. 

The four designs chosen for evaluation, the birdcage design, Alderman & 

Grant design, split-ring resonator, and the saddle coil were all constructed 

with the same diameter (7.5cm) and length for direct comparison. The criteria 

chosen to evaluate the performance of each design included the probe 0-factor 

(loaded and unloaded), the effect of sample on the probe resonance frequency 

and the homogeneity of the rf magnetic field inside the probe. In addition, 

the signal-to-nolse ratio and the 90 ° pulse width for a "point" phantom were 

also determined. 

Experimental results obtained indicate the relative merits and demerits of 

different probe designs. In summary, it is seen that higher 0 values are 

afforded by the resonator probe designs (birdcage, Alderman-Grant and 

split-ring) and that the split-ring resonator gives the best results. In 

general, the dielectric losses associated with the resonator probes are lower 

than that of the saddle coil, and the Alderman-Grant design provides the best 

performance with respect to this parameter. Qualitative estimates show that 

the resonators generate higher inductive losses compared to the saddle coil. 

The best rf homogeneity in all three axes is provided by the split-ring 

resonator. The rf homogeneity of the saddle coil is comparable to that of the 

Alderman-Grant design in the transverse plane and the former offers better 

performance along the longitudinal axis. 

127 I HETERONUCLEAR TWO-DIMENSIONAL NNR METHODS FOR THE DETERM]NATION 

OF THE PRIMARY STRUCTURE OF PEPTIDES 

VoLker Bornemann, A. Scott Chesnick, Gregory Helms, Richard E. 

Moore and Walter P. Miemczura* 

Department of Chemistry, University of Hawaii, Honolulu, HI 96822. 

The common method of determining the primary structure of peptides and 

small proteins using RMR spectroscopy involves a combination of homonuctear 

experiments in both protonated and deuterated solvents. These experiments are 

generally the most straight-forward method for solving this problem. There are 

several drawbacks to this approach. Data must be obtained in the presence of 

protonated solvents. Also, key information is obtained from proton-proton nOe 

experiments which can be weak or sometimes absent due to chemical exchange. Finally, 

the method breaks down for non-standard amino acids such as beta amino acids or those 

which are chemically modified. Recently the improved sensitivity of modern 

spectrometers and the introduction of proton detected direct and long-range 

heteronuctear chemical shift correlation experiments has opened a whole new avenue 

towards solving the problem of peptide sequencing with NNR spectroscopy. Now 

hitherto unavailable information concerning the direct and remote connectivities 

between carbon or nitrogen and hydrogens can now be obtained on reasonable quantities 

of material. With the aide of tow level isotopic enrichment (ca 1OX uniform N-15 

throughout the molecule) even carbon-nitrogen correlations can be determined. Our 

work involves the isolation and identification of biologically active natural 

products from blue-green algae. In many instances these compounds are peptidat in 

nature. Because of the modified nature of these molecules the standard NNR 

sequencing techniques are often inadequate. We have found that a broad range of not 

only homonuclear but also heteronuctear experiments are often needed in order to 

completely characterize these new compounds. By combining direct and tong-range 

correlation of carbon and nitrogen to protons with carbon-nitrogen correlation 

experiments it is possible to determine the primary sequence of peptides using one 

end two bond correlation experiments. We will present two recent peptidat compounds 

which could not be sequenced with homonuctear two-dimensional experiments due to 

structural modifications or ambiguous homonuctear data. For both of these compounds 

the availability of data from the heteronuclei was essential in solving the unknown 

structures. ALl information wilt be provided for the experiments presented. ]n 

addition, hardware and probe modifications necessary for performing the carbon- 

nitrogen correlation experiments wilt be discussed. 

162

I-- 1 2 8 IVOLUME-SELECTIVE SIGNAL SUPPRESSION IN SURFACE-COIL NrMR 

SPECTROSCOPY: COMPARISON OF THREE METHODS. C.D. Smith, G.S. Thomas, S.L. Smith*, 

Magnetic Resonance Center, University of Kentucky, Lexington, KY 40506 

We compared the radio-frequency (RF) field profile of a 3.0cm 31p-tuned surface 

coil, using three methods to suppress signal close to the coil while collecting 

signal from deeper regions. These methods are: (I) Bendal's depth pulse using both 

first order and second order elimination, (2) spatially-selective prpsaturation with 

low-power pulses, and (3) Erst-angle optimization (in a surface coil, this amounts to 

a second form of spatially-selective presaturation). The latter two methods may be a 

useful "poor man's" alternative to gradient or multiple coil technique for collecting 

in vivo 31p spectra of brain, with reduced contamination from overlying muscle, for 

example. The basis of comparison is intensity ratio of the signal profile at 

critical distances from the coil. 

Experiments were performed on a Spectroscopy Imaging Systems VIS 4.7 tesla 

system, oeprating at 81MHz for phosphorus. The surface coil was placed perpendicular 

to a 0.5cm rectangular slab phantom containing 3M sodium dihydrogen phosphate 

(T 1 = .Is); this form for the sample makes slice selection gradients unnecessary for 

imaging. Images of the RF profiles and associated intensity traces, plotted to the 

same scale and window settings to aid visual comparison, are highly instructive and 

will be presented. Advantages and disadvantages of each method for in vivo 

applications are discussed. 

- - 12 9 I!N VIVO VOLUME LOCALIZED SURFACE COIL SPECTROSCOPY WITH ISIS AND 

DRESS: THE CHEMICAL SHIFT DISPLACEmeNT. C.D. Smith, G.S. Thomas, and S.L. Smith* 

Magnetic Resonance Center, University of Kentucky, Lexington, KY 40506 

A problem in gradient volume selection spectroscopy, dependent directly on main 

field strength, is the chemical shift effect, which can be summarized as follows: 

the volumes from which signal is collected for individual lines in a spectrum are 

displaced in space, the displacement proportional to their chemical shift. This 

means, for e::ample, two peaks in a single rat brain 31p spectrum may originate from 

opposite hemispheres. Some spectral lines may be attenuated or absent because the 

corresponding volumes lie outside the brain entirely. 

In DRESS the selected volumes consist of displaced parallel planes with centers 

.,eparated by distance S, in centimeters, S = o • Bo/g " 102 , where O is the 

separation in parts per million between spectral lines of interest, Bo is the main 

field in Tesla and g the gradient strength in gauss per centimeter. The gradient 

effect on chemical shift is negligible. 

In the ISIS experiment, selected voiumes consist of a diagonally displaced stack 

of cubes corresponding to each line; the overlap in volume between the cubes depends 

both on gradient strength and pulse bandwidth. With some combinations of these, the 

volumes may not overlap at all. For example, in a 4.7 tesla system at phorphorus 

frequency with a nominal ma::imum gradient strength of 2.0 gauss/cm, the distance 

between centers of cubes corresponding to opposite ends of a typical spectrum is 

0.94cm. The effect is significant when considering localization to volumes of this 

order= e.g., rat brain. Nuclei with a large chemical shift range, e.g., carbon, 

su~er greatest with the phenomenon. Spatial variation of metabolic parameters, e.g., 

phosphorylation potential, over a range of centimeters must also be considered in 

interpretation of spectra obtained using these methods; the assumption of tissue 

homogeneity over this range should be included in such interpretations. We wi!7. sho~ 

in vivo spectra obtained using ISIS and DP~SS demonstrating the above considerations. 

163

130 I 

SEQUENTIAL ASSIGNMENT OF AMIDE PROTONSIN o~-HELICES IN LARGE PROTEINS 

Steven W. Sparks +*, Ad Bax ++, and Dennis A. Torchla + 

NIDR +, NIDDK++,National Institutes of Health, Bethesda, MD 20892 

We describe an approach that yields sequential assignments of proton signals in u-helices in 

proteins that are too large to apply the standard assignment strategy. Deuteration of 

non-exchangeable protons is used to enhance dNN connectivities in the protein NOESY spectrum, 

thereby revealing long sequences of dNN connectivities that are characteristic of (x-helices. Double 

labeling with 13C/15N is used to edit and assign signals in proton detected heteronuclear shift 

correlation (HMQC) spectra of the protein. The sequential assignments are obtained by comparing 

i 

the amide proton chemical shifts in the NOESY and HMQC spectra. We show that this meihod 

provides assignments for all amide protons in the three (x-helical domains of staphylococcal 

nuclease complexed with pdTp and Ca 2+, MW = 18 kDa. The fact that the assignments were obtained 

at a low protein concentration (1.5 raM), and at physiological temperature (36.5 °) and pH (7.7), 

indicates that this approach can be applied to a wide range of proteins. The HMC)C spectra also 

provide assignments of protons outside of the (x-helices. We show that these assignments can be 

used as starting points for sequential assignments of other structural domains in the protein. 

131 

f 

MASS TRANSFER PROCESSES STUDIED BY NMR IMAGING. 

L.D.HALL AND A.G.WEBB* 

Laboratory for Medicinal Chemistry, 

Level 4, Radiotherapeutic Centre 

Addenbrookes Hospital, Hills Road, 

Cambridge. CB2 2QQ. England. 

Diffusional processes play an important role in many chemical and 

biological systems. Examples include the rate determination of chemical 

reactions, and the mass transport properties of biological membranes. NMR 

imaging can be used to follow these processes by exploiting the difference in 

relaxation properties between the species of interest and the medium through 

which it is diffusing. Quantitative information concerning diffusion 

coefficients can then be calculated. 

We will present examples of the diffusion of common solvents through 

industrially important polymers such as polymethylmethacrylate. In addition we 

have studied the temporal and spatial localisation of the aerially catalysed 

reduction of hydroquinone to produce a semiquinone anionic free radical. This 

series of radical anions play an important role in various biological pathways. 

All experiments were carried out on an Oxford 2T wide-bore ( 31 cms. ) 

magnet. The maximum gradient strength of lOmT/m produced a slice thickness of 

3.5mm. An inversion recovery spin echo refocussed imaging sequence was used to 

produce T 1 weighted images. 

164

-- 

is 2 I 

NATURAL ABUNDANCE 13 C and 14 N NMR OF BACTERIAL OSMOLYTES IN VlVO. B.A. 

Lewis,~'S.C.Cayley, S Pedmanabhan, and M.T. Record, Jr. Dept. of Chemistry, 

University of Wisconsin, Madison Wl 53706. 

Bacteria such as E. Coli and _5. Typhimurium are capable of growing under conditions of moderately 

high osmotic stress, up to about 0.7 molar salt. To adapt to such high-osmolarity environments, the bacterial 

cell accumulates potassium ions and also synthesizes or accumulates one or more small organic molecules. 

These include the anion glutamate and the neutral or zwitterionic molecules praline, glycine betaine ( N,N,N- 

trimethyl glycine) and/or trehalose, a glucose dimer. Because these small molecules are~ccumulated to 

intracollular concentrations on the order of 0.5 molal, they are readily observed in dense cell slurries by 

natural abundance 13 c NMR on our Bruker AM360 with a I 0 mm broadband probe. 14 N NMR is also useful to 

observe glycine betaine, which has a relatively narrow 14 N spectrum due to the symmetric environment of 

the nitrogen and its lack of exchangeable protons. 

We are able to measure the relative and absolute amounts of the various organic osmolytes accumulated 

by the bacteria in viva under a variety of environmental conditions. In minimal medium with 0.5 M NaCl, 

trehalose and glutamate are the only small organic molecules present in high amounts. If I mM praline is added 

to the medium, it is accumulated to nearly 0.4 M intracellularly, with some diminution of the trehalose and 

glutamate levels. 61ycine heroine, however, also supplied at I mM, is accumulated to about 0.5 M, and 

trehalose is completely eliminated. 

Under these high salt conditions, significant amounts of rf power are absorbed by the sample, 

particularly at the high frequencies of 90 MHz for 13 c and 360 for I H. Thus for the i 3 C experiments we 

employ gated proton dacoupling to minimize sample heating. In addition, the pulse lengths must be calibrated 

for each sample, and internal standards must be used for quantitative measurement. 

-- 133 ! 

CHARACTERIZATION OF HUMAN BLOOD PLASMA USING VERY HIGH FIELD 

DIFFEERENCE SPECTROSCOPY. 

Dadok, J.*, Bothner-By, A. A., Mishra, P.K., Carnegie Mellon 

15213 

Wilkinson, D. A., Giles, R. H., Acevedo, H. F., Shrivastava, 

Allegheny-Singer Research Institute, Pittsburgh, PA 15213 

RESOLUTION ENHANCED PMR 

Univ., Pittsburgh, PA 

P.N., Jarmillo, B., 

Blood plasma from cancerous patients was compared with plasma from healthy males and 

females using 620 MHz PMR spectra with various degrees of resolution enhancement. The 

variations in the content of VLDL, LDL and HDL as well as of other plasma components 

was evaluated with the use of difference spectroscopy. Preliminary results indicate 

that this technique may provide useful information on the physiological state of the 

blood plasma. We could see also systematic and substantial differences in plasma of 

healthy males and females and we feel that comparison should be made within well de- 

fined groups of the same sex. 

References: 

I. Fossel, 

2. Bell, D. 

Letters, 

E.T., Carr, J.M. and McDonagh, J., N. Engl. J. Med.,315 1369-1376 (1986). 

J., Sandler, P. J., Macleod, A. F., Turner, P. R., LaVille, A., FEB 

219, 239-273 (1987). 

165

V FERFUSION PROBE FOR A BRUKER AM-400 WIDE-BORE SPECTROMETER. 

134 J Mark E. Anderson e# , Michael #Chob a ni an A, Ed S. Mooberry ~. John L. 

Markley # and Carlos Ar~s ~. National Magnetic Resonance Facility 

at Madison and Department of Biochemistry, College Of AAgriculture and Life Sciences, 

University of Wisconsin-Madison, Madison, Wl 53706. University of Wisconsin, 

School of Medicine, Madison, WI 53792, ~b Department of Biochemistry, Autonomous 

University of Barcelona, Barcelona, Spain. 

We constructed a probe for the Bruker AM-400 wide-bore spectrometer that 

permits the perfusion of kidney proximal tubules. The design was inspired by the 

work of Y. Boulanger, et al., but we chose a solenoidal coil geometry and doubly- 

tuned the probe to P-31 and H-2 [1]. The deuterium channel facilitates the shimming 

of the uncommon geometry. Since the proximal tubules of the kidney are very oxygen- 

dependent, flow rates on the order of 200 ml/min are necessary in a perfused system. 

The probe's design permits flow rates up to 1,000 ml/min. The construction of the 

perfusion chamber permits easy sample access and minimizes the chances for leaks and 

disruptions of coil geanetry. The temperature is monitored by a thermocouple 

located in the effluent side of the perfusion chamber. We have tested the system 

and have found that it is possible to maintain cell viability for over 12 hours. 

The proximal tubules are isolated and injected into hollow dialysis fibers that are 

then inserted into the perfusion chamber. The ATP levels of the cells rose to a 

steady state value after two hours of perfusion and remained at those levels for the 

duration of the experiment. With this system and modifications to the electronics, 

a wide range of metabolic experiments of sensitive cells are possible. 

[1] Y. Boulanger, P. Vinay, M.T. Phan Viet, R. Guardo and M. Desroches, Magn. Reson. 

Ned. 2, 495-500 (1985). 

[Supported by: U.S.-Spain Joint Grant CCA-8510/098, NIH grants RR02301 and RR027gl, 

NSF Grant PCM-84504g, NKF 133M007, the U.S. Department of Agriculture, and the 

University of Wisconsin.] 

BO,~IONUCLEAR TWO DIMENSIONAL saC DOUBLE GUANTUM CORRELATION 

V SPECTROSCOPY (2D xJC[x~C]DOC) AND IH-{13C]HETCOR AS PRIMARY TOOLS 

135 J FOR SPIN SYSTEM AND HE~ ASSIGNmeNTS IN CYTOCHROME Csss: Michael 

D. Reilye, Eldon L. Ulrich, William M. Westler and John L. Markley, Department of 

Biochemistry, College of Agricultural and Life Sciences, 420 Henry Mall, University of 

Wisconsin-Madison, Madison, WI 53706. 

The first step in sequence-speciflc resonance assignments, identification of 

individual spin systems, has traditionally involved time-consuming acquisition and 

analysis of several 2D experiments that correlate scalar-coupled proton networks. We 

present an alternative method for spin system identification that relies mainly on 

scalar a3C-IsC and I~C-IH coupling. The IJC[ISC}DOC experiment is first used to 

assign carbon spin systems. Next, the IH[13C]HETCOR experiment is used to extend 

these assignments to carbon-bound proton resonances. Amide and amine NH resonances 

are then identified and sequential assignments made by XH(I:C)MR-HECTOR(HMBC) or a 

combination of NOESY and COSY. This approach has several advantages over proton- 

proton methods. First, there are eighteen unique amino acid xsC-IsC coupling patterns 

and only eight unique IH-IH spin systems. Second, primary assignments are based on 

conformation-independent one-bond 13C-I~C and x:C-ZH connectivities. Proton methods 

rely on dihedral-angle-dependent three bond coupling, and so expected cross peaks may 

be weak or nonexistent. Third, proteins have fewer carbons than protons, and these 

have a larger chemical shift range~ this simplifies analysis for larger proteins or 

for proteins that have a significant amount of random coil structure. Fourth, xJC-IsC 

connectivities currently provide the only general means of making unambiguous aromatic 

side chain assignments. Finally, the new method reduces the time needed for resonance 

assignments. Isotope-enriched proteins can be obtained inexpensively by the use of 

modern blotechnology methods. We demonstrate the technique for cytochrome csss from 

Anabaena 7120 uniformly labeled to 26% in I~C. Computer programs are being developed 

to automate first and second order assignments based on these data. [Supported by 

USDA 85-CRCR-1-1589, NSF PCM-g4504g and NIH RR02301, RR02781.] 

166

. ° 

THREE-DIMENSIONAL STRUCTURE OF TURKEY OVOMUCOID THIRD DOMAIN BY 2D- 

136 J NMR SPECTROSCOPY, AND DISTANCE GEOMETRY CALCULATIONS. Prashanth 

Darba , Andrzej grezel, ~asna Fejzo, S. Macura, Andrew D. Robertson 

and 3ohn L. Markley, National Magnetic Resonance Facility at Madison and Department of 

Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin- 

Madison, Madison, WI 53706. 

Turkey ovomucoid third domain (OMTKY3) is a small 56-residue protein that inhibits 

serine proteinases. Previous studies [1,2] based on chemical shift differences have 

revealed that subtle changes in the tertiary structure occur near and remote from the 

cleavage site upon hydrolyzing the reactive-site peptide bond. Recently 247 inter- 

proton distances were determined from a series of 2D-NMR experiments. Some of the 

distances were estimated crudely from the number of contour levels of well resolved 

peaks in a single NOESY spectrum; others were determined accurately from a set of 

NOESY/ROESY experiments obtained with 7 different mixing times. [3] 

These NMR distance constr'aints were used in two different distance geometry 

programs, DG900 [4] based on a metric matrix approach and DISMAN [5] which uses a 

variable target function, to determine the solution structure of OMTKY3. A comparison 

of the structures calculated from these methods with the X-ray structure of OMTKY3 [6] 

will be presented. Implications of crude versus accurate distances on the structure 

determination and convergence properties of the two distance geometry programs will be 

discussed. 

[1] A.D. Robertson, W.M. Westler, and 3.L. Markley, Biochemistry, in press. [2] G.I. 

Rhyu and J.L. Markley, Biochemistry, in press. [3] 3. Fejzo, S. Macnra, and 3.L. 

Markley, unpublished data. [4] 3. Thomason, M. Day, and I.D. Kuntz, nA Vectorized 

Distance Geometry Program, n in prep. [5] W. Braun and N. Go, 3. Mol. Biol. 186, 611- 

626 (1985). [6] R.$. Read, M. Fujinaga, A.R. Sielecki, and M.N.G. James, Biochemistry 

22, 4420-4433 (1983). 

[Supported by: NTH Grants RR 02301 and GM 35976 and the University of Wisconsin- 

Madison.] 

I 

-- TWO-DIb~ENSIONAL xIC(XSN}, x3C{x3C} AND XH{x3C} CHEMICAL SHIFT 

137 I CORRELATION IN PROTEINS: SI~UENCE-SPECIFIC ASSIGN~[ENT OF 

RESONANCES IN xsC AND XSN LABELED S.TREPTOMYCES SUBTILISIN INHIBITOR. William M. 

Westler, *~ M. Kainosho, # H. Nagao, # N. Tomonaga,# and 3ohn L. Markley ~. ~Department 

of Biochemistry, College of A~ricnltural and Life Sciences, University of Wisconsin- 

Madison, Madison, WI 53706. ~Department of Chemistry, Faculty of Science, Tokyo 

Metropolitan University, Fnkazawa, Setagaya-ku, Tokyo, 158 Japan. 

Applications of heteronuclear two-dimensional NMR to proteins and other 

macromolecules are proving to be extremely useful for resonance assignments in large 

proteins. Here we demonstrate the use of two-dimensional shift correlation methods 

between ssC and ISN, ssC and IsC, and aH and ssC for determinin 8 sequence-specific 

assignments in Streptomyces snbtilisin inhibitor (SSI). Two-dimensional ssC{SSN} 

correlation spectroscopy is used to detect coupling between selectively ssC labeled 

methionine ssC o resonances at position i in the protein sequence and the SSN labeled 

amide peak of the next sequential residue (i+1) in [ul 60% SSN, 99% a3C o methionine] 

SSI. The known assignments of the methionine xsC o peaks allow sequence-specific 

assignment of the XSN a peaks of the i+1 amino acid residue We also report here a 

novel method for sequence-specific assignments of carbon and proton resonances in xsC 

labeled proteins by the use of 3 two-dimensional methods: xsC[s3C} double-quantum 

correlation, SB(ssC} one-bond chemical shift correlation, and SH{ssC] multiple-bond 

correlation. By these methods, the NMR spin system assignments of the nine lencine 

residues in [85% ul s3C]leucine SSl are extended from the previously assigned 

carbonyl carbons to the intraresidne alpha carbons, alpha protons, and to the alpha 

protons of the next sequential amino acid. [Supported by Grants in Aid from the 

Ministry of Education of Japan (60430033, 60880022, 62220026), NIH grants RR02301 and 

RR02781, NSF Grant PLM-845048, the U. S. Department of Agriculture, and the 


167

[ 1 3 8 J FERREDOXIN FROM ANABAENA 7120 : UNIFORM CARBON-13 AND/OR 

NITROGEN-15 ENRICHMENT AND NUCLEAR MAGNETIC RESONANCE INVESTIGATIONS 

Byung Ha Oh% _ William M. Westler, Prashanth Darba and John L. Markley0 

Department of Biochemistry, 420 Henry Mall, University of Wisconsin-Madison, 

Madison, WI53706. 

Uniformly carbon-13 (28%) and/or nitrogen-15 (~9b~) enriched ferredoxin (plant 

type, 2Fe-2S*) were obtained by growing Anabaena 7120 (a cyanobactertum) with 

26% x3C CO 2 and/or )95% XSN KNO~ as the sole carbon and/or nitrogen source. By 

applying two-dimensional (2D) ssc[x3C} double-quantum correlated spectroscopy 

(xsC{xSC}DOC) to the uniformly xsC enriched ferredoxin, the carbon spin systems 

of 75 of the 98 amino acid residues in the protein were identified and 

classified by the amino acid type. Most of the carbon spin systems that were 

not observed probably correspond to amino acid residues near to the paramagnetic 

center. The striking feature of this experiment is the ease of arC spin system 

analysis: the data set was analyzed in about a week. Because xH-xsC groups can 

be assigned via the xR detected xsC experiment, this approach provides an 

efficient way for analyzing xH spin systems. "sC{XSN] heteronuclear correlated 

spectroscopy (xsC[XSN}RETCGR) applied to [ul 26% xsC, ul )95% XSN]ferredoxin 

revealed Co/N cross peaks from 83 of the peptide bonds and 6 side chains (Gin, 

Ash). By applying the x3C{xSC}DOC and ssC{XSN]RETCOR experiments, it should be 

possible to obtain sequential assignments along the pepttde backbone with a 

single dual xsC/XSN labeled protein. These two novel 2D experiments which 

exploit direct one-bond coupling, represent a new methodology for assigning 

protein NblR spectra. [Supported by USDA Competitive Research Grant 85-CRCR-1- 

1598, NIB Grant RR02301, NIH Grant RR02781 and NSF Grant PCg-845048.] 

TWO-DIMENSIONAL HYDROGEN-1 NUCLEAR MAGNETIC RESONANCE STUDIES OF 

159 1 STAPHYLOCOCCAL N~CLEASE: SPIN SYSTEM ASSIGNMENTS IN THE (NUCLEASE 

B124L) "DEOXYTHYMIDINE-3 ' ,5 '-BISPHOSPHATE" CA2 + TERNARY COMPLEX 

Jinfeng Wang and John L. Markley, National Magnetic Resonance Facility at Madison 

and Department of Biochemistry, College of Agriculture and Life Sciences, University h 

of Wisconsin, Madison, WI 53706 

Two-dimensional NMR methods have been used to assign resonances from the 

aromatic and a substantial number of non-aromatic residues in the XH NMR spectra of 

the staphylococcus aureus V8 variant nuclease ternary complex: (nuclesse H124L)" 

deoxythymidine-3',5'-bisphosphate'Ca z+. Specific assignments are presented for all 

14 of the aromatic spin systems. The assignment methods used relied heavily on the 

two-dimensional NMR experiments. The aromatic ring resonances were identified by 

combining ROHAHA, COSY, and NOESY experiments. Ambiguities in distinguishing 

between phenylalanine and tyrosine spin systems were resolved by making use of 

sequential backbone assignment of two unique dipeptide segments in the primary 

structure of staphylococcal nuclease, and by comparison of NOE data with the 

structure derived from single crystal X-ray diffraction. 

Heteronuclear two-dimensional NMR studies have assisted the assignments and 

provide more information for detailed analysis of the conformation of nuclease 

H124L in the presence and absence of pdTp and Ca 2+. 

[Supported by Nil] Grant GM35976 and NSF Grant DMB 84-10222; NMR studies were 

supported by NSF Grant PCM-845048, NIH Grants RR02301 and RR02781, the USDA and the 


168

~-'-- 140 

DIRECT OBSERVATION OF LONG RANGE HETERONUCLE~ SPLIETINGS IN 

• PROTON 2DJ SPECTRA: T. K. Pratum, P. K. Hammen* and N. H. 

] Andersen, University of Washington, Seattle WA 98195 

Pr0ton-detected heteronuclear 2DJ-resolved experiments have been designed 

a/_lo~ring the observation of long range heteronuclear couplings (nJcH). Placement 

of a 180 ~ carbon pulse at the midpoint of the hon~nuclear 2DJ evolution period pr~ah~ces 

a signal n~dulated by both heteronuclear and hamonuclear coupling. Selective 

detection of protons ~rith long range coupling to 13C nuclei surmounts the inherent 

d C~p'ul c r~l~Be difficulty encount~d with proton dete.ct.ion. For this selection the 

se at the nlidpoint of t I is n~Ddulated or an additlona_l n~ulated 180 n C_I 

pulse is placed either at the end of t I or at the beginning but a fixed, (2 JCH ) , 

delay a~ter the initial proton 90 ° pulse. %~nese lead to differs_noes in the signal 

detected, and corLsequently in data presentation. Of them the most useful sequence 

, ,2 "* I I "'* 

IH I I Acq(e.) 

In this case, a 45 ° projection of the 2D data matrix elindnates proton J couplings 

preser~ring the long range heteronuclear couplings. A~litude reduction of the mod- 

ulated 13C pulse, nmk/_ng it sendselective for a desired sl~ect-ral region, pr~)vides 

another advantage. It elind_nates all but the couplings to the selected carbons 

which is beneficial when several couplings exist with nearly identical n~gnitude. 

%~nese metheds have been developed ~sing ar~m~itic an~o acids as test systems 

• ~rith selective 13 C edifying in the carbonyl region. %~ne experiment has been extend- 

ed to l~=-ptides where it provides a means for assigning diastereotopic methylene 

protons and deter~dzling the side cha/in dihedral angles. 

141 I BRANCH LOCATION STUDIED BY SOLVENT SWELLING AND SOLID 

STATE NMR IN ISOTOPICALLY ENRICHED ETHYLENE-I-BUTENE COPOLYHERS: 

D. HcFaddin, Queen's University, Kingston, Ontario, Canada. K7L 3N6 

Homogenous ethylene-l-butene copolymers (isotoplcally enriched 

at the methyl group) have been studied by solid state NHR, as a 

function of crystallization conditions and comonomer content. Two 

enviror~nents are seen for the branches Ln all cases. 

Ln the solution crystallized samples the methyl region of the 

spectrum is characterized by two broad overlapping peaks. However, 

the addition of excess solvent (carbon tetrachloride) causes an 

increase in the mobility of the amorphous chains and improved 

resolution in the methyl region of the spectrum. The solvent does 

not penetrate the crystalline regions of the polymer and therefore 

only effects the amorphous branches of the sample. 

In a 0.2 tool% sample (crystallized from the melt) 

approximately 18% of the branches reside in a restricted region, 

while 37% of the branches exist in a crystalline-like (non-swollen) 

region in the solution crystallized polymer. In a 2.5 mol% sample 

approx~ately 12% (melt crystallized) and 22% (solution 

crystallized) of the total branches exist in this crystalline-like 

(non-swollen) region of the polymer. These sidechains are probably 

located in a defective crystalline overlayer. 

169

142 ] 

TRANSITIONS: 

Laboratory, 

INDIRECT DETECTION OF 14N ~M=2 (OVERTONE) NMR 

A. N. Garroway* and J. B. Miller, Naval Research 

Code 6122, Washington D. C. 20375-5000 

For quadrupolar spin systems in high magnetic field, 

the ~M=2 NMR transition is weakly allowed, due to the slight 

distortion of the pure Zeeman states by the quadrupolar 

perturbation. For such overtone transitions, the theory and 

direct observation of the 14N resonance, occurring at about twice 

the 14N Larmor frequency, have been already presented by other 

workers. Here we extend the method by using the IH spin system 

to detect indirectly the nitrogen overtone transition. First IH 

dipolar order is created and then progressively destroyed by 

repetitive contacts with the nitrogen rotating frame Zeeman 

reservoir; we monitor the loss of the IH signal. The 14N 

irradiation is stepped in frequency during the cross-relaxation 

to compensate partly for the reduced effective 14N rf field 

strength. The merit of the indirect over the direct detection 

scheme is the corresponding increase in signal intensity. We 

demonstrate 14N indirect detection methods on some crystalline 

solids including hexamethylene tetramine. 

14 3 I DIFFERENTIAL DEVELOPMENT OF MULTIPLE-QUANTUM COHERENCE IN A 

LIQUID CRYSTAL: W. V. Gerasimowicz*l", A. N.Garroway, and J. B. Miller, Chemistry Division, Code 

6122, Naval Research Laboratory, Washington, D. C. 20375-5000. 

A 2:1 molar mixture of 4'-cyanophenyl-4-n-heptylbenzoate and 4'-cyano-phenyl-4-n- 

butylbenzoate exhibits nematic liquid crystal behavior in the temperature range from 25 o 

to 50o C. The proton NMR spectra suggest that two regimes of dipolar interaction are 

present L e. those characteristic of partially-isolated proton spin pairs, presumably on the 

phenyl rings, and weakly-coupled spins originating from the alkyl chain moieties 

comprising the remainder of the system. A solid-echo pulse sequence permits the 

observation and separation of these unique regions within the molecules on the basis of 

their differing relaxation properties. We have combined this technique with multiple- 

quantum NMR, so that the spins are first prepared by means of a variable delay solid-echo 

sequence followed by MQ NMR experiments. Differential development of proton spin 

coherence can then be distinguished (in this case) for different segments of the same 

molecule. We find that over the course of the multiple-quantum preparation times, the 

phenyl proton pairs do not interact appreciably with the remaining protons of the molecule. 

1"Permanent Address: U. S. D. A., Eastern Regional Research Center, 600 E. Mermaid Lane, 


170

144 I 

I IH AND 13C REFOCUSED GRADIENT IMAGING OF SOLIDS 

J. B. Miller* and A. N. Garroway 

Naval Research Laboratory, Code 6120 

Washington, DC 20375-5000 

We have previously demonstrated a technique for removing 

distortions from NMR images due to chemical shift and susceptibility 

effects which we call refocused gradient imaging (RGI). The technique 

relies on the Carr-Purcell pulse sequence to refocus the chemical- 

shift-like evolution of the spins. The sign of the gradient is 

switched synchronously with the rf pulses so that gradient evolution 

is not refocused. 

Here we extend refocused gradient imaging to the observation of 

solids. For high natural abundance spins where the homonuclear 

dipole-dipole interaction dominates, the Carr-Purcell sequence is 

replaced by a pulse sequence which simultaneously refocuses the 

dipolar and chemical-shift-like interactions. For low natural 

abundance spins the Carr-Purcell sequence is used. Where necessary, 

high power decoupling of heteronuclei may be added. 

We describe the pulse sequences used for RGI of solids and show 

examples of both IH and 13C images. The relative merits of IH and 

13C RGI are discussed. We find that because of differences in 

experimental parameters and more efficient line-narrowing for 13C RGI, 

the low natural abundance of 13C is not a severe limitation for carbon 

imaging of solids. 

145 I 

DERIVATION OF POLYMER RI~IEOLOGICAL CONSTANTS 

FROM THE VISCOSITY AND TEMPERATURE DEPENDENCE OF xsC NMP. 

RELAXATION PARAMETERS: Anita J. Brandolini, Mobil Chemical 

Company, Edison Laboratory, P.O. Box 240, Edison, New 

Jersey 08818 

NMR relaxation parameters characterize polymer chain 

motions on a local scale; theological constants describe 

the viscoelastic properties of a bulk material. 

CorrelatinE bulk property measurements with spectroscopic 

data enables one to determine the contribution of local 

seEmental reorientations to overall chain motions. The 

IsC NMR llnewidths of low molecular-weight 

polyisobutylenes exhibit power-law dependences on sample 

viscosity. The exponent, which is different for each 

carbon type (quaternary, methylene, and methyl), specifies 

the fractional contribution of each carbon type to the 

polymer's free volume and monomeric friction coefficient. 

Furthermore, the IsC NMR linewidths have a 

Williams-Landel-Ferry (WLF) dependence on temperature, 

which is the same form observed for the temperature 

variation of many bulk viscoelastic properties. The 

derived values for free volume and thermal expansion 

coefficient aEree with published rheological parameters to 

within ±10%. 

171

146 I SO~ APPLICATIONS OF THE ~TR EXPERI~IENT: Dallas L. Rabenstein, 

Uei Guo and Erin Smith, Department of Chemistry, University of 

California, Riverside, California, 92521. 

In the WATR (w_ater ~ttenuation by T__ 2 r_elaxation) experiment, the 

water resonance is eliminated by selectively decreasing the spin-spin 

relaxation time of the water protons by chemical exchange and then 

measuring the spectrum by the Carr-Purcell-Meiboom-Gill (CPMG) pulse 

sequence.l, 2 With this method, the water resonance can be selectively 

eliminated and resonances at the chemical shift of the water resonance 

can be observed. In this poster, we describe several applications of 

the WATR method, including measurement of IH-NMR spectra of peptides in 

99% H20/1% D20 , observation of resonances for protons bonded to 

natural-abundance15N in peptide bonds, and measurement of IH-NMR 

spectra for aqueous samples, including biological fluids. Resonances 

for protons on the a-carbons of peptides are normally obscurred by the 

water resonance, however they are readily observed by the WATR method 

and can provide useful information in studies of the chemistry of peptides, 

as will be illustrated by results from studies of the 

thiol/disulfide chemistry of peptides. 

I D.L. Rabenstein, S. Fan and T.T. Nakashima 

541 (1985). 

J. Magn. Reson., 64, 

2 D.L. Rabenstein and S. Fan, Anal. Chem. 58, 3178 (1986). 

147 

-- I THERMALLY INDUCED VOLUtlE CI~NGES IN A BLOCK COPOL~IER: Franco Cau* 

Serge Lacelle, D~partement de chimie, Universit6 de Sherbrooke, Sherbrooke, Quebec 

CANADA JIK 2R1 

Recently some temperature induced molar volume changes have been reported for 

solutions of block copolymers of propylene oxide (P) and ethylene oxide (E) with 

structures of the type (E) _ (D) - E (i). We have studied the expansibility of a 

m n o 

- P - with IH T I and lineshape as a function of the 

polymer solution of El00 44 El00 

temperature and concentration. The resonances of the E and "D monomers are well 

resolved thereby permitting to monitor the microscopic environments in the different 

blocks of the Dolymer. Our findings include I) the volume changes can be associated 

with the P block, 2) determinatio~3of the overlap threshold concentration, 3) the 

radius of Ryration scales with N ~ , where N is the degree of polymerization. These 

results will be discussed in the light of various scalinE behavior (2). 

i. R.K. ~Jilliams, H.A. Simard, C. Jolicoeur, J. Phys. Chem. 89, 179, (1985). 

2. P.C. de Gennes, Scalin~ Concepts in Polymer Physics, Cornell U. Press 1979.

~ 

(POSTER ABSTRACT) BARBARA LYONS/CORNELL UNIVERSITY 

CHALLENGES TO THE CLASSICAL MODELS OF REACTIVITY 

148 I The possibility of heavy atom tunneling, in this case that of 

carbon atoms, has been investigated through calculational methods by several different 

researchers in recent years. However, the molecules of interest used in the calculations 

of these researchers have not been readily feasible as models for study in the 

laboratory. To test the theory of heavy atom tunneling a suitable molecule needed to bE 

found: one which would lend itself to available laboratory techniques. We turned to the 

molecule semibullvalene as a possibility, due partly to its startlingly low energy of 

activation(5.5+0.1kcal/mol at -140°C). 

Semibul~alene undergoes a degenerate cope rearrangement at room temperature. The 

classical'~C isotope effect for the rearrangement at -170°C is k../k.~=l.04. However 

~ 1~ 

by performing a simplistic quantum mechanical calculation we preozcted that, including 

tunneling contributions, the isotope effect for semibullvalen~3at -170°C should be 

about kl2/k =2 8 The k value is determined from the fully C subst, molecule. 

3 " " 13 

To test t~zs hypothesis we turned to variable temperature n.m.r.line-shape analysis 

using a 400 MHz spectrometer. Spectra were taken of the natural abundance molecule fro~ 

-160°C to -35°C in 3°C increments. Likewise, after the all C molecule had been synthesized, 

spectra were taken in the same temperature range. A two-site exchange model 

was used on a mainframe computer to calculate the relevant n.m.r, line-shapes for each 

temperature. This gave us the rat~_constants for the natural abundance molecule. 

However, upon comparing the all~3C spectra to the ~tural abundance spectra by overlap 

plotting an unpleasant fact was noticed. The all--C line-shape width for each temperature 

was the same as the natural abundance line-shape width for that same temperature. 

Unfortunately only one conclusion was possible: that the fullyl3c molecule had 

virtually the same rate constants at any given temperature. Therefore, in at least the 

temperature range we were looking at, tunneling was not a major contributing factor 

to the reaction process. 

149 

I 19F NMR STUDIES OF FLUORINE SUBSTITUTED Ba2YCu307_ x 

C. E. Lee*, D. White, P.K. Davies, J. A. Stuart 

University of Pennsylvania, Philadelphia, PA 19104 

Gaseous phase exchange has been used to introduce substantial 

concentrations of fluorine into orthorhombic perovskite powder 

samples. The temperature dependence of the NMR lineshape and 

signal amplitude in the normal and superconducting states are 

presented for several fluorine concentrations. In general, it is found 

that the presence of the oxy-fluoride phase does not significantly 

affect the superconducting transition temperature of the bulk 

sample, but does decrease the extent of field exclusion, i.e., the 

Meissner effect of the bulk powder. Some preliminary spin lattice 

relaxation data are presented in which the 19F NMR is used as a 

probe of the electronic environment of the oxide in the normal and 

superconcucting states. 

173

-- 150 I ISOTOPE DETECTED NOE EXPERIMENTS ON 13C LABELED tRNAPhe: William 

H. Gmeiner*and C. Dale Poulter, Department of Chemistry, University 

of Utah, Salt Lake City, UT 84112 

Isotope directed and isotope detected nuclear Overhauser effect experiments are 

performed on tRNA^ ne from E. coli in which all the adenine residues were labeled at 

position 8 with ±jC. The experiments are used to establish the presence of the 

unusual Hoogsteen type base-pair in the solution structure of the molecule. A 

relaxation p~file of the lab~edlsite is presented in which the effect of two 

quadrupolar --N spins on the -C- H spin system is analyzed. The rel~ation effect 

on the imino proton of uridine in adenosine-uridine base-pairs by the--C label is 

used to measure the relative populations of Watson-Crick and Hoogsteen base-pairs in 

a chloroform soluble model system. 

- - isi 

I 

Inversion Recovery Cross Polarization (IRCP) techniques are used to probe the 

structures of morphologlcally different polyethylenes. Crystalline and amorphous 

components were resolved by their different cross polarization (CP) rates which were 

discriminated by an IRCP pulse sequence. At least two major magnetically distinct 

environments were detected in each sample. The arystalllne-amorphous interfaclal 

domains were also detected in some samples. The cross polarization time, TCH, of 

each phase was compared among these morphologically different samples and can be 

interpreted in terms of structural details. 

The effect on TCH by varying magic angle spinning speed and spln-lock power 

were also studied. The chemical shift anlsotropy (CSA) of each component and the 

degree of crystalllnlty of these semicrystalllne polymers were also discussed in the 

study. 

174

1 52 I ~IR STUDY OF NAPHTHALENE TRANSPORT AND P~ELA)LATIOtq IN THE NAPHTHA- 

LENE-SUPERCRITICAL ETIIYLENE SYSTEM: K. W. Woo , S. Adamy and J. Jonas, University 

of Illinois, Urbana, IL 61801 

The purpose of this study is to investigate the motional dynamics of naphthalene 

in the naphthalene-ethylene supercritical mixture using T 1 and diffusion measurements. 

The deuterium TI for d,-naDhthalene were measure'd along three isotherms 

_ _o . i . o -. . , . f 

(lu, 30, 4J C) in the solld-supercrltlcal ethylene ohase at pressures rom i00 to 

i000 bar, and along two isotherms (70, 78°C) . from 20-200 bar for the liquid naphtha- 

lene-suoercritica] ethylene phase. The pressure dependences of the relaxation rate 

of d_-naohthalene in the two phases show quite a different behavior. In particu]ar, 

tile effect of dissolved ethylene dominates tile motional characteristic of naphthalene 

in the liquid naphthalene phase. In order to complement the data, the diffusion 

coefficients of naphthalene were also measured using tile fixed-field gradient Bessel 

• function analysis technique. The experimental data are interpreted in terms of 

current theoretical models. A brief discussion of tlfe potential of i,~ techniques 

to orovide unique molecular level information on suDercritical fluid systems is 

also included. 

NMR CHARACTERIZATION OF THE SOLUTION, GEL AND 

153 SOLIDS STRUCTURES OF [(I-3)-~-D-GLUCAN (CURDLAN)] 

P. H. Bolton and P. J. Giammatteo*, Wesleyan 

University, Middletown, CT and A. J. Stipanovic, Texaco Research 

Center, Beacon, NY, 12508 

Naturally occuring microbial polysaccharides represent an 

important class of compounds whose characteristic properties are 

used in applications ranging from foods to enhanced oil recovery. 

While typically composed of one to five simple sugars per repeat 

unit, polysaccharides can exhibit complex tertiary structure such 

as single, double and/or triple helices. Through hydrogen 

bonding and/or cross-linking mechanisms, these systems can form 

interchain networks. Further, varying degrees of crystallinity 

can result depending on both the monomeric makeup and the 

linkages betweeen monomers on the polysaccharide. Depending on 

precipitation, hydration and/or solution conditions, Curdlan, 

[(l-3)-~-D-Glucan], a linear homopolymer of glucose, can exist in 

one of three distinct solid structures, can form thermally 

setting gels, or can exist in either a triple or single helix in 

solution. CP/MAS 13C NMR was used to study the solid and gel 

forms and a variety of 2D solution NMR experiments were employed 

to elucidate the molecular conformation, 

| • • 

self-assoclatlon 

mechanism and gel domain structure of Curdlan. All experimental 

procedures and applications will be presented and discussed. 

175

-- 154 I 

DISCRIMINATION BETWEEN SYMMETRIC AND ASY~9~ETRIC HYDROGEN BONDS BY 

ISOTOPIC PERTURBATION OF EQUILIBRIUM. Charles L. Perrin and John 

D. Thoburn*, Department of Chemistry, University of California, 

San Diego, La Jolla, California 92093. 

The method of isotopic perturbation of equilibrium was used to 

distinguish symmetric and asymmetric hydrogen bonds in monoanions 

of two carboxylic acids. Oxygen-18 substituted maleic and succinic 

acids were prepared by hydrolyzing their respective anhydrides with 

H2180. The 13C resonances of these acids as well as their dianions 

in aqueous solution show an intrinsic isotope shift of 0.027 ppm. 

Titration with KOH to the monoanion of succinic acid produces an 

increase in chemical-shift difference to 0.048 ppm, which is at- 

tributed to an asymmetric hydrogen bond. The mmleic acid monoanion 

shows no such increase in chemical-shift difference, demonstrating 

that its proton lies in a symmetric single-well potential. This is 

a general method which can be used to~stinguish between symmetric 

and asymmetric hydrogen bonds in a wide variety of systems. 

155 I 

NMR STLIDIES OF PHOSPHATIDYLCHOLINES AND THIOPHOSPHATIDYLCHOL]NES 

Mufeed H. Basti* and Laurine A. LaPlanche 


Northern ]11inois University 

DeKalb, II. 60115 

The substitution of a sulfur atom for oxygen in the polar head 

group of dioctanoylphosphatidylcholine causes siqnificant 

differences in the NHR spectrum of the two phospSolipids. 

Three-bond proton-proton, phosphorus-carbon and phosphorus- 

proton coupling constants for groups near to the sulfur (oxygen) 

atom indicate conformational differences not only in the polar head 

group region but also in the glycerol portion of the two molecules. 

Chemical shifts of nearby proton and phosphorus nuclei are also 

affected by the substitution. The methylene protons adjacent to 

the sulfur atom in the thio-analogue exhibit magnetic nonequivalence 

at both 200 and 500 HHz, while those of the oxygen analogue are 

equivalent. 

Results are analyzed in terms of population differences betweer, 

preferred conformations of phosphatidylcholine and thiophospha- 

t idylchol ine. 

o o~o" l 

o 

176 

o 0,, xo" . 

o

is6 I 

ROTATING FRAME COHERENCE TRANSFER DUE TO TUNNELLING 

Eric R. Johnston Haverford College Haverford, PA 19041 

Slow tunnelling of protons and heavier atoms in chemical reactions is a 

subject of considerable interest but the unambiguous demonstration of it is 

difficult. Unlike thermally activated chemlcal exchange (which randomly averages 

chemical shift differences) tunnelling coherently averages such differences and 

its effects in NMR are expected to be quite different from those due to exchange. 

In particular in the Hennig-Limbach rotating frame exchange experiment (i) the 

tunnelling frequency should appear not in the decay rate of the spln-locked 

magnetization but as an oscillation imposed upon the decay (2). Moreover, 

tunnelling is expected to be invisible in selective inversion transfer exper- 

iments in contrast to chemical exchange. 

The theory describing these effects is briefly d¢scussed and experiments 

illustrating them are presented. We have employed coherent spin decoupllng as 

a (mathematically equivalent) model for a tunnelling process in experiments on 

an AX spin system which involve spin locking of the X doublet components in the 

presence of weak resonant decoupling of the A spin. The question of proton 

tunnelling in tetraphenyl porphine (TPP) ~s cr~t~cally addressed ~n light of o6r 

results and the possibility of employing a spin locking experiment to detect 

slow tunnelling is assessed. 

i. J. Hennlg and H. H. Limbach, J. Ma~n. Reson., 49, 322 (1982). 

2. E. Johnston, J. Magn. Reson., in press (July, 1988). 

157 

ldllclnomlldn-1 

+4 5 "It, 

+ INTACT STRUCTURE. OF ACLACINOMYCIN-A 

n,~_J+3B_~L~_~g~, I 

Satish Arora § and Mohan CharP 

* Department of Chemistry, Rice University, Houston, Texas 77254; 

§ College of Pharmacy, DDI, University of Texas, Austin, Texas 75712; 

+~ Baylor MRI Center, Woodlands, Texas 77381 

04 $' l - llllilsUlll~l 

4 '.,- -" '+-"- 

- 140 0~_'+~.~041 5" 

2 " j'+ i" "0 

.... 177 

TI~ InU~ ~ amit~e ol ms sr~l~o~ ,~la¢l'mmycln-A, has l~en 

obu~l bY • o~mblnsllon ~ nwllnuci~ ~ aml 3-I) compumr OraI)PEs 

Im:hn~ues. Thedsgmmtl~dlsolON, al-~L.1 donoldemonstr~oa 

COml~miy ac~rste oonlornationaJ pl~Jm of mls molscul, whk:~ Is 

now In actlve dlrlCal ~mls. Desl~) ths fact thal thls molecule exhb~ 

an extmmsly elflck)r0 mlaxatlon Woomm~ {'r t's ~; 0.75 seconds) due to 

the ~ side ctw~. tho solution structure of Adaclncmyc+n-A 

l.m been ol~n~l.."¢~c/non"yc+n~ undo rg ~s a ~ cl°l~nci~ 

I~¢utat, Mff-a~clatl~ d ms ak/vlnone slmlelon dngs. They 

mack ,xtl-,ogonally wl~h ors snomw and c~,,.,, an Imom'~ol~lar o~chw',,go 

o+ lablle l't~Irogsrl fmm ttw 4,.OH and 6-OH PC61tlons. "Tllm~ Is 

mymallogralmiC evideme for tits In the I:mm~

158 I SOME TRICKS OF THE TRADE FOR BETTER 2D NMR SPECTRA 

( ou comment monter une mayonnaise ~ la main . . ) 

Dominique MARION *+ and Ad BAX 

Lab. of Chemical Physics N.I.D.D.K. 

BETHESDA MD 20892 U.S.A. 

N.I.H. 

The information content of most 2D NMR experiments, in the context of 

conformational analysis, is presently underestimated, since several expe- 

rimental imperfections still prevent one from interpreting the more subtle 

pieces of information actually present in the spectrum. In any 2D map re- 

corded in the phase sensitive mode, improper phase correction as well as 

baseline rolls are major concerns for correct quantification of the spec- 

tral parameters. On the basis of the pulse phases and durations and delays, 

the necessary phase corrections can be computed ab initio, avoiding the 

waste of time caused by trial-and-error iterative correction. By a proper 

setting of the experiment, the phase correction can even be minimized 

before acquisition. Similarly, the apparently irreproducible baseline dis- 

tortions, which originate in part from an incorrect quantification of the 

first data polnt(s), can be rationalized and thus minimized. These features 

will be illustrated on the conformational study of maEainin (I), a 23-re- 

sidue antimlcrobial peptide from the frog skin. 

(I) D. Marion, M. Zasloff and A. Bax (1988) FEBS Lett 227:21 

(+) on leave from the Centre de Biophysique Mol~culaire Orldans France 

159 I 

DEVELOPMENT OF FLUORINATED, NMR ACTIVE SPIN TRAPS FOR 

STUDIES OF FREE RADICAL CHEMISTRY: Barry S. Selinsky , Louis A. Levy, 

Ann G. Motten, and Robert E. London, National Institute of 

Environmental Health Sciences, Research Triangle Park, NC 27709. 

The use of spin traps, nitrone or nitroso compounds which react 

with free radicals leading to the production of thermodynamically 

stable spin adducts, has greatly enhanced the detection of reactive 

radicals by electron spin resonance. Five fluorinated analogs of the 

spin trap phenyl-tert-butyl nitrone (PBN) have been synthesized and 

evaluated for use as NMR active traps. The introduction of the 

fluorine substituent allows selective observation of chemical re- 

actions involving the spin traps. Althoug~_the paramagnetic adducts 

themselves are not directly observable by ~F NMR as a consequence of 

extensive broadening, the reduced forms (hydroxyl amines) can be 

readily observed. The series of 2-F, 4-F, 2,6-F 2-CF_, and 4-CF 3 

substituted PBN analogs have been synthesized. The'relative trapping 

efficiencies of the synthesized spin traps were tested by reaction 

with known concentrations of phenyl radical generated from phenyl-azo- 

triphenylmethane in benzene. In addition, the trapping efficiencies 

of 2,6-F 2 PBN and 2-CF~ PBN relative to unsubstituted PBN could be 

compared due to significant differences in ESR proton hyperfine 

coupling constants of their phenyl adducts. The fluorinated spin 

traps synthesized here could potentially be useful in in vivo studies 

of biological free radicals, where reduction of nitroxides makes ESR 

analysis difficult. 

IZ8

16 0 I A 27AL MAS STUDY OF AMORPHOUS ANODIC ALUMINA: STRUCTURAL 

INFORMATION COMBINED WITH QUANTITATIVE UNCERTAINTY. *I. Farnan (1)t, R. 

Dupree (1), M.E. Smith (1), Y.S. Jeong (2) and G. Thompson (2). (1) Physics Department, University 

of Warwick, Coventry CV47AL, U.K.; (2) Corrosion and Protection Centre, UMIST, Manchester 

SK97AL, U.IL 

The ability of 27A1 MAS-NMR to distinguish between aluminium in different coordination 

states in aluminas and aluminosilicates has been known for some time. Here the technique is ap- 

plied to technologically important amorphous anodic aluminas whose structures are poorly known. 

The study reveals five-fold coordinated aluminium in these materials in addition to the more usual 

aluminium coordinations of four and six, all with a symmetry comparable to crystalline alumi- 

nas. The film formation conditions are observed to influence the relative amounts of this quasi- 

crystalline aluminium observed in the spectrum. 

Because of the range of bond lengths and angles in these amorphous materials there re- 

mains a broad contribution to the spectrum associated with aluminium electric field gradients 

which are not averaged by MAS. As well as causing un-narrowed lines in the spectrum, electric 

field gradients can cause the aluminium signal to be broadened beyond detection, or not to be excited 

by the RF pulse. This results in the need to compare signal intensities with a standard in order to 

establish the fraction of the aluminium in the sample which is represented by the NMR spectrum. 

Signal fractions for anodic alumina films together with signal fractions for crystalline materials 

with known electric field gradients are presented. The amount of aluminium signal varies de- 

pending on the anodizing conditions and the electrolyte used, which can be related to the film mor- 

phology observed by electron microscopy. 

t Present address: Dept. of Geology, Stanford University, Stanford, California 94305-2115 

_ _ 

r 

161 I 

LOCALIZED PROTON SPECTROSCOPY AND SPECTROSCOPIC IMAGING OF THE HUMAN BRAIN 

* Peter Luyten and Jan den Hollander 

Philips Medical Systems, PO Box i0.000 

Best, The Netherlands 

We have developed and optimized a pulse seouence to obtain localized 

watersuppressed proton spectra in the human brain. By combining selective 

excitations with phase encoding gradients one dimensional spectroscopic imaging 

could be performed, resulting in the simultaneous aquisition of watersuppressed 

proton spectra from different slices through the human brain. Slice selective 

excitation pulses were given in three orthogonal directions. Two directions 

restrict the volume of the slices and one direction parallel to the phase encoding 

direction suppresses the very intens signals of subcutaneous fat and bone marrow. 

These signals may obscure the metabolite resonances with.~n the same chemical shift 

range. Volume selection was achieved by stimulated echo's. Watersuppression was 

obtained by binomial pulses and selective dephasing pulses. Using this sequence 

spectra can be obtained showing well resolved resonances of choline, creatine, 

N Acetyl Aspartate and lactate in the submillimolar range. Studies are in progress 

to examine cerebral infarcts and brain tumors in patients ............... 

179

162 I 

HIGH RESOLUTION IOC-IH SHIFT CORRELATION WITH FULL [H-IH DECOUPLING. 

163 I 

M. PERPICK-DUMONT, *a W.F. REYNOLDS a AND R.G. ENRIQUEZ, b DEPARTY~NT OF 

CHEMISTRY UNIVERSITY OF TORONTO AND INSTITUTO DE QUIMICA, Utah7 ...... zDAD 

AUTONOM~ DE M~XICO. 

A COLOC-like sequence combined with a selective BIRD refocussinz 

pulse is used to generate fully IH-IH decoupled 13C-IH shift correlated 

spectra with F 1 line widths of ca. 7Hz. The sequence is generally freer 

of artifacts and more sensitive than earlier sequences measured under 

comparable conditio:=s. A minor modification of the sequence, which 

allows simultaneous observation of IJcH couplings, is particularly 

useful for determination of small differences in IJcH for non-equivalent 

CH 2 groups. IH chemical shifts and IJcH couplings can be measured with 

a precision of < iHz, except in cases of strongly coupled CH 2 groups. 

However, even in these cases, it may still be possible to de:ermine 

very small chemical shift differences by simolation-of ~' ~ 

_LI~ non--first 

order behavior. 

laC AND *SN MASS SPECTRA OF LABELED 

STAPHYLOCOCCAL NUCLEASE CRYSTALS 

Holly B.R. Cole* and Dennis A. Torchia 

NIDR, National Institutes of Health, Bethesda, HD 20892 

Osing genetically transformed E. Coli (provided by 

Professor John Gerlt), we have labeled staphylococcal. 

nuclease (Nase), an 18 kDa enzyme , with a variety of 

selectively enriched amino acids. We report MASS spectra of 

Nase, labeled with [methyl-lee] methionine and [15N] valise. 

Lyophilized Nase has relatively broad, poorly resolved lines 

indicating local disorder. In contrast, crystalline Nase has 

well resolved lines whose chemical shifts may be compared to 

Nase chemical shifts observed in solution. This technique 

provides the means to compare protein structures in the 

crystalline and solution states using the same experimental 

parameters. In addition, because of the high sensitivity and 

resolution of the MASS spectra, one has the opportunity to 

study protein internal dynamics at numerous assigned single 

atomic sites in the protein crystals. 

180

164 

I MODIFICATIOH OF A BRUKER WH-300 SPECTP.OI~TEP. FOP. 

B.~OADBAI[D/nlGd POWER SOLID STATE IR~ EXPEP.II~E~ITS 

Virgil Simplaceanu (*) and Chien Ho 

Department of Biological Sciences, Carnegie Mellon University 

4400 Fifth Avenue, Pittsburgh, PA 15213 

A modification is described that allows performing broadband/high power I~ 

experiments on a commerci~l spectrometer originally designed for high resolution 

I~. in liquids. 

Additional P~F gating and four phase channels are provided, gated by a timing 

simulator under the control of the Aspect computer. One RF channel has amplitude 

control capability for spin locking experiments and can also be used for shaped pulse 

applications if driven by an arbitrary waveform generator. A !lenry ~adio tunable i kW 

amplifier and/or a 50W broadband ENI amplifier are used as transmitters. The standard 

preamplifier is replaced by a fast mecovery, non-saturating preamplifier. 

Full compatibility and easy switchover from standard configuration to high power 

and back is maintained. The standard Bruker ~. software can be used to control the 

execution of (automated) experiments via microprograms. 

165 I 

/ , / 

IN VIVO PHOSPHOROUS-31 NMR STUDIES OF HUMAN BRAIN AT 1.5T 

~aplan D. # , Pa,chalingam K. + McEvoy J. +, Spiker D. +, Keshavan M.S.+, Wolf GE #, Pettegrew J. 4-- 

"The Pittsburgh NMR Institute, 3260 Fifth Ave, Pittsburgh, PA 15213 

+Western Psychiatric Institute and Clinic, 3211 O'Hara St., Pittsburgh, PA 15213 

We have studied the dorsal prefrontal cortex in eight human subjects by 31p NMR. All studies were 

conducted on a General Electric Signa Scanner coordinating both imaging and spectroscopic protocols. 

Spectroscopic localization within the prefrontal cortex was achieved by surface coil B 1 profiling, and confirmed 

by proton imaging. Peak areas were calculated for phospho-monoesters, ortho-inorganic phosphate, 

phospho-dicsters, phosphocreatine, and the nucleotide phosphates via a computerized spectral deconvolution 

program yielding a simulated spectrum of Iorentzian lines with frequencies, linewidths, and areas 

corresponding to the experimental spectrum. The observed values from normal adult volunteers, given in 

mole percent, are as follows: PME = 15.9, Pi = 8.06, PDE = 38.65. PCr = 11.15, gamma-ATP (ionized 

ends) = 9.44, alpha-ATP (esterified ends) = 9.89, beIa-ATP = 6.86. These values yield the f¢~llowing 

ratios: PME/PDE = 0.41, PCr/P i = 1.38, PCr/ATP = 1.62. These results compal" ~ very well to both 

classical biochemical assay of freeze clnmped extracted mammalian brain, as well as "P NMR studies of 

freeze-clamped exhacled mammalian brain. 

These results suggest that in vivo NMR spectroscopy of adult human brnin conld provide metabolic 

insights into neuropsychiatric diseases. Schizophrc,ia, in particular, would be particulnrly applicable since 

both structural and metabolic alterations of the dorsal prefrontal cortex have been implicated. 

181

SOLID STATE NMR STUDY ON THE STRUCTURE OF GRAMICIDIN A: Teng, Q., 

155 I North, C.L., Brenneman, M.T., LoGrasso, P.V. and Cross, T.A., Department of 

Chemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-3006. 

Gramicidin A is a fifteen amino acid polypeptide that forms a cation selective channel in natural and 

synthetic membranes. Structural information is being derived from solid state NMR studies of gramicidin 

in hydrated lipid bilayers. 13C and 15N labeled gramicidins have been synthesized both by biosynthesis 

with Bacillus brevis and by solid phase peptide synthesis. Extensive lipid bilayers containing gramicidin 

are studied both as oriented and unoriented preparations. Solid state 15N chemical shift and dipolar spectra 

are analyzed to yield bond orientations for determining the polypeptide backbone torsion angles. 

Furthermore, limitations on the N-H bond lengths in this polypeptide are presented. These solid state NMR 

experiments provide basic information for the calculation of the gramicidin A channel structure. 

[ 

~ DYNAMICS OF THE GRAMICIDIN A TRANSMEMBRANE CHANNEL BY 

1 67 [ SOLID STATE 15N NMR: L.K. Nicholson, M. T. Brenneman, P.V. LoGrasso and 

T.A. Cross, Florida State University, Institute of Molecular Biophysics and 

Department of Chemistry, Tallahassee, Florida 32306. 

The dynamics of specific sites in the peptide backbone of the gramicidin A cation selective- 

transmembrane channel have been studied using solid state 15 N NMR. Gramicidin A is a polypeptide 

consisting of fifteen amio acids which dimerizes to form a single stranded helical pore in a lipid bilayer. 

Its generally accepted structure is the ~6.3 helix which, due to the uniquely alternating L/D amino acid 

sequence places the hydrophobic side chains on the outside of the channel where they interact with the 

hydrocarbon core of the bilayer, and the polar peptide linkages along the interior of the channel which 

enhances solvation of the channel ion. Although gramicidin is the most extensively studied channel, an 

atomic resolution mechanism of ion transport is not known. Characterization of motions of various groups 

within the channel backbone will help to elucidate the specific interactions that result in transport of the ion 

across the membrane. Motions of specific sites along the channel backbone have been detected by observing 

the averaging of the lSN chemical shift anisotropy (CSA) tensor as a function of temperature in both oriented 

and unoriented samples. It has previously been shown that fast overall channel rotation occurs in and 

above the lipid phase transition region, and that the axis of rotation coincides with the channel axis which is 

parallel to the bilayer normal. This global rotation becomes slow on the 3kHz timeframe of the NMR 

experiment when the temperature is below the onset of the phase transition. Recent studies of the temperature 

dependence of the l SN spectra of both oriented and unoriented samples show evidence for local motions of the 

peptide linkages existing above the onset of the gel to liquid crystalline phase transition, and that the 

amplitude of these motions varies along the channel backbone. These local motions have a large amplitude 

at the monomoer - monomer juction where the peptide linkage planes contribute a proton to the hydrogen 

bonds linking the two monomers. The temperature dependence of oriented samples where yield a very 

sharp resonance above the phase transition region has proved to be a very sensitive indicator of dynamics 

when the temperature is lowered. The resonance linewidth below the phase transition reflects directly on the 

range of orientations swept out by the dynamic process at higher temperatures. This new tool for assessing 

dynamics should have broad application in systems that can be oriented. 

182

IN VIVO 31p AND IH NMR SPECTROSCOPY AND IMAGING 

I-- OF RAT LIVER EXPOSED TO HALOCARBONS 

1 68 IRheal A. Towner$, Manfred Brauer*t, David Foxallt, and Edward G. Janzent. 

Guelph~Waterloo Centre for Graduate Work in Chemistry, Department of Chemistry and 

Biochemistry, University of Guelph, Guelph, Ontario, Canada NIG 2WI; $ Spectroscopy 

Imaging Systems Corp., 1120 Auburn St., Fremont, California USA 94538. 

Intoxication by hepatotoxins such as carbon tetrachloride (CCI~) is characterized 

by centrilobular necrosis and fatty degeneration of the liver. The specific damage to 

the liver is directly related to the metabolism of CCI~ by the liver. 

3~p-NMR in vivo spectroscopy was used to demonstrate metabolic changes in rat 

liver as a function of time after exposure to either CCI~ or bromotrichloromethane 

(BrCCI3). The inorganic phosphate peak shifts upfield which is associated with a 

decrease in cytosolic pH. CCI~ or BrCCI3 intoxication causes an intracellular acidosis 

to pH 7.02 or 6.80 (±0.05), respectively. Also, it has been found that halocarbon 

exposure alters the relative amounts of phosphomonoesters and phosphodiesters detected. 

CCl~ and BrCCI3 induced changes which were readily detectable by NMR imaging 

techniques. Respiratory gating was used to attenuate motion artefacts due to 

breathing, and standard transverse multi~slice images were obtained on a SIS 200/330 

system (TE 18 ms). Two to four hours after the administration of either CCI~ or 

BrCC1 a, regions of high signal intensity appeared in the rat liver images. These 

affected areas were in the region where the portal vein enters the liver. Localized 

~H NMR spectra, using the VOSY technique, indicated that the high proton signal 

intensity was due to water, rather than a localized fatty infiltration. T 2 

determinations of the water resonance within the affected regions of the liver showed 

a significantly longer water T2 relaxation time than unaffected areas of the liver. 

Interestingly,3the administration Of halothane anesthetic alone produced very similar 

results. These studies indicate localized tissue damage, with cell rupture and 

release of intracellular water. (Financial support from the Univ. of Guelph 

MRI Facility, University of Guelph.) 

; 169 

SPECTROSCOPY WITH EXACT APODIZATION TRANSFORMATION ( SWEAT ); 

M. Lisicki, A. A. Bothner-By, R. Shukla, J. Dadok, P.C.M. van Zijl, 

Carnegie Mellon University, Pittsburgh, PA., 15213 

The finite discrete Fourier Transform applied to a theoretical time 

function of infinite duration produces frequency domain spectra distorted by 

truncation effects (sync wiggles) which interfere with precise spectral 

measurement. For example, doublet splittings determined by measuring the 

frequency separation between line maxima will be incorrect if the sync 

wiggles from one llne produce a significant slope at the maxima of the other 

line. 

On the other hand, a line shape created in the frequency domain will 

have a unique inverse transform. The inverse transform of this novel line- 

shape used as an apodization function will produce the exact desired llne 

shape in the experimental spectra once the natural line shape has been 

removed from the experimental fid. The removal of the natural llne shape 

can be accomplished by using the inverse transform of a singlet in the 

experimental spectra which contains the desired natural line shape. 

We will demonstrate the application of deconvolution and line-shape 

generation using exact apodization. Furthermore, we will show their use in 

exact spectral measurement. The computer program SWEAT which will implement 

these techniques will be available. 

18S

170 ] 

FLOW-COMPENSATED NMR IMAGING TECHNIQUES FOR RHEOLOGY OF 

SUSPENSIONS 

P.D. Majors, S.A. Altobelli, E. Fukushima, Lovelace Medical Foundation, Albuquerque, N.M. 

87108., and R.C. Givler, Sandia National Laboratories, Albuquerque, N.M. 87185. 

A suspension is a mixture of solid particles in a viscous fluid. Many natural processes (e.g., 

blood circulation and river sedimentation) and industrial processes (e.g., transport of slurries and 

filtration) are affected by the properties of suspensions. Unforttmately, there is a dearth of rhe- 

ological information for suspensions at ILigh concentrations due to limitations suffered by most 

measurement teclmiques. NMR yields spatially resolved quantitative velocity mid particle density 

information. 

We used flow-compensating NMR imaging techniques to determine the flow properties (fluid 

and particle velocity distributious, particle density distribution) of viscous suspensions. Constituent 

concentrations for flowing two-phase systems can be obtained by time-averaging the resonant signal 

of, say, the fluid phase. The concentration of the second phase is thus inferred from the 'reduced' 

fluid signal. Preliminary NMR studies of two-phase stationary and flowing systems demonstrate 

the quantitative nature of the tecludques with good sensitivity and resolution. 

RAPID ROTATING FRAME IMAGING WITH RETENTION OF CHEMICAL SHIFT 

INFOP~MATION .~ M #* 

171 J P.M. Macdonald ~, K.R. etz , J.P. Boehmer + 

#Radiology Department, New England Deaconess Hospital, Harvard Medical School, 185 

Pilgrim Road, Boston, MA 02215 

+Department of Internal Medicine, University of Massachusetts Medical Center, 55 Lake 

Avenue North, Worcester, MA 01605 

Rotating frame imaging (RFI) is an elegant and simple technique for mapping the 

spatial distribution of NMR spectral information (I). The image is formed by using a 

homogeneous static field B and an rf field gradient B.(x) generated with a surface 

coil. Spins in different s~atial regions exhibit nutatlon frequencies u I which are 

proportional to the rf field strength: Ul=YBl(X)/2~. In Rapid RFI, whic~ is several 

orders of magnitude faster than conventional RFI, the spectral line of interest is 

)laced on-resonance and a single FID of n points is acquired (2) using: 

Preparation - (Pulse - Acquire One Point) - Relaxation. 

[DFT then produces an image relating spin density and nutati~nal frequency (spatial 

distribution). Unfortunately, spatial information from off-resonance signals remains 

intermixed. 

Our approaches to removing the undesired signals include: a) selective +90 vs -90 ° 

tipping of the signal of interest using DANTE such that the difference image contains 

only the desired information, b) P~I with and without selective inversion using shaped 

pulses (3) in order to eliminate extraneous signals using subtraction, and c) removal 

of off-resonance contributions by virtue of their fast decay in the Rapid RFI sequence. 

(I) D.Hoult, J.Magn.Reson. 33, 183 (1979). 

(2) K.Metz and J. Boehmer, J.Magn. Reson., submitted. 

(3) M.Silver, R.Joseph, and D.Hoult, J.Magn.Reson. 59, 347 (1984). 

184 ....

. r 

172 JMAGIC ANGLE SPINNING SEPARATED LOCAL FIELD SPECTROSCOPY: SOME 

EXPERIMENTAL OBSERVATIONS RELEVANT TO THE DETERMINATION OF C-H DISTANCES BY NMR: 

Gretchen G. Webb* and Kurt W. Zilm, Department of Chemistry, Yale University 225 

Prospect Street, New Maven, CT 06511 

The calibration of the homonuclear scaling factor is very important in 

obtaining accurate results for 13C-IH bond distances by separated local field 

spectroscopy (SLF). It has generally been noted that the best fits of SLF data always 

give an effective scaling factor that is significantly less than that measured on a 

standard liquid sample if C-H distances from diffraction studies are used to calculate 

the dipolar couplings. This discrepency has been attributed by other workers to the 

effects of molecular motion or alternatively interpreted as indicating that C-H 

distances are in fact longer than measured by either neutron or x-ray diffraction. In 

this paper the problems with calibrating the homonuclear scaling factor in CPMAS 

probes is discussed and it is suggested that scaling of 1H-13C J couplings for a 

liquid sample may be the most accurate approach. Using this technique the scaling 

factor for a semi-wlndowless MREV-8 sequence is found to be that predicted by theory. 

When the scaling factor is determined from HAS SLF patterns the scaling factor is 

found to always be reduced by the same amount if C-H bondlengths are assumed to be 

1.09 A. This reduction in the scaling factor occurs for both CH and CH 2 groups and is 

apparently independent of temperature down to 77K. The results indicate that molecular 

and lattice libratlons are the principal sources of the reduction in observed dipolar 

couplings. 

~ --- 173 I 

Determination of H-H Bond Distances in Transition Metal Dihydrogen Complexes 

by Solid State NMR 

M. Chinn, M. Cozine, M. Heinekey, G. Kubas, t J. Millar*and K. Zilm 

Dept. of Chemistry, Yale University, New Haven, CT 06511 

1"Los Alamos National Laboratory, Los Alamos, NM 87545 

Molecular hydrogen (H 2) somewhat surprisingly acts as a ligand in a large number of transition metal 

complexes LnM(Vl2-H2 ). These complexes are of great interest to the organometallic community since they 

may model an intermediate in the oxidative addition of H 2 to form dihydrides. Not surprising is the fact that 

the interaction of the H 2 ligand and the metal exhibits a wide degree of variation depending on the metal and 

the basicity of the ligands, L. In the simplest model, stronger binding of the H 2 by the metal should result in 

lengthening of the H-H bond. These distances have been studied by techniques such as x-ray and neutron 

diffraction as well as by solution 1H T 1 measurements. We report measurements of H-H distances by a 1H 

solid state selective pulse method which suppresses the homogeneous lineshape of the ligands, L, and 

allows observation of the H 2 dipolar Pake pattern. These Pake patterns are complicated by torsional 

oscillations of the H 2, but study of the lineshapes as a function of temperature in most cases leads to models 

for the motion and allows determination of the H-H distances..In the Mo, Ru and W complexes studied to 

date, observed powder pattems are -500 kHz in width, indicating bond distances ranging from 0.89 to 1.02 

Angstroms. 

185

It 

174 I 

DESIGN OF A HIGH RESOLUTION HIGH PRESSURE DOUBLE RESONANCE 

NMR PROBE: P. J. Grandinetti', D. Vander Velde, C.-L. Xie, N. A. Walker, and 

J. Jonas, University of Illinois, Urbana, IL 61801 

High pressure NMR studies have demonstrated the importance of pressure in under- 

standing molecular dynamics in liquids. We have extended this technique to study 

complex disordered systems using double resonance (i.e. x3C{1H}) NMR at pres- 

sures from 1 to 4000 bar. The new design minimizes the length of rf transmission 

hnes between the sample coil (in the high pressure environment) and the resonant 

circuit (in the ambient environment). The sample coil is double-tuned so that large 

sample volumes (12 mm diameter) can be used within the pressure vessel for cases 

of low sensitivity. 

Prehminary results are reported for a study of the pressure effects on the molecular 

motion of 2-ethyl hexylbenzoate, a model synthetic elastohydrodynamic lubricant. 

175 

CARBON-13 CP/MAS NMR STUDY OF THE NYLON-6 POLYMOPHS AND DYNAMICS: 

Dehua Wang',Jianzhi Hu, Xin Yan, Guoxi Wan9 and Baogon9 Qian, 

Wuhan Institute of Physics, Academia Sinica, Wuhan, Hubei, P.R. China 

C-13 CP/MAS spectra of nyton-5 were obtained on MSL-400 instrument. 

was foundthat the ~ carbon 

has two peaks in 

originate from d 

in sotution spec 

existence of dif 

state the = , p 

A series o 

contact time to 

feast square opt 

potarization rat 

a 15 ~' 5 

- [-CO-CH= -CH= -CH= -CH, -CH= -NH-] -. ny t on-6 

sotid state. They are designated as ~ = and ~ , which 

ifferent crystattine components. The two peaks coatesced 

tru= of the same sampte. It 9ires the evidence of co- 

ferent crystattine re9ions in sotid nyton-6.In the sotid 

eak is 2.2 ppm to upfietd from the ~ • peak. 

f CP/MAS spectra of nyton-6 was measured by varyin9 the 

investigate the dynamic behavior. A SIMPLEX nontinear 

imization at9orithm was apptied to catcutate the cross- 

es T,, and the proton T• p . The dynamic parameters of 

sotid nyton-6 we re catcutated accordin9 to Ngai formatism. 

186

2 

. ° 

I- 

176 I 

Michael A. Kennedy and Paul D. Ellis 


University of South Carolina 

Columbia, South Carolina 29208 

SING~.CRYSTAL NMR STUDIES OF II3cD COMPLEXES 

AND --SCD NMR OF CADMIUM PROTOPORPHYRIN IX AND 

CADMIUM MYOGLOBIN. 

For the past ~eral years, we have been involved in establishing a 

understanding of ~Cd NMR chemical-shift-structure correlations throug 

single crystal oriented NMR experiments. A major impetus for thes 

studies has be~ 3 the desire to interpret chemical shift tenso 

information for Cd substituted proteins. In the absence of adequat 

single crystals, one must rely on trends established through singl 

crystal experiments for interpretation. In the case of oxocadmiu 

complexes, the following has been established; i) the least shieldeq 

element is aligned most nearly perpendicular to the plane containin, 

water oxygens, ii)two tensor elements having similar values must havq 

similar orthogonal environments, iii) in the absence of water oxygen 

the deshielded element is oriented to maximize the short-bond oxygel 

shielding contribution, and iv) the most shielded element is most nearl' 

perpendicular to the longest cadmium-oxygen bond. The results o 

investigation of some mixed cadmium-oxo-nitrogen complexes and cadmium 

oxo-halogen ~plexes will be presented here. 

Also, Cd solid and solution state NMR for i) cadmium 

protoporphyrin IX dimethyl esterl13a model complex for cadmium-myoglobil 

and cadmium-hemoglobin, and ii) Cd-myoglobin will be presented an, 

discussed. This work was supported by the National Science Foundation 

grant #CHE86-11306, and the National Institues of Health, grant #GM26295 

- - 177 

I 

Beth Crockett and Paul D. Ellis 



Columbia, South Carolina 29208 

~E ADSORptiON OF Rb + AND Cs + TO TRANSITION ALUMINAS BY 

"Rb AND ---Cs SOLID STATE NMR SPECTROSCOPY 

8~ecently, in this lab, Cheng and Ellis have shown the effects on 

the Rb I solid state nmr of varying coverages of RbCl adsorbed on 7- 

iAlumina. Through this work, the following conclusions have been made: 

IFirst, there are at least four different species present on the surface 

fat sub-monolayer coverages of RbCl. Secondly, going from lower to higer 

Icoverages corresponds to a relative decrease in the rate of growth of 

the surface species compared to th~ salt specles. And thirdly, the 

Rb ion motion in the interstitial sites 

~ resence of water facilitates 

f the surface, giving credence to the idea of adsorbate islanding. 

In work to be presented here, we intend to show the effects of RbCl 

and CsCI adsorbed onto aluminas with varying surface areas. These 

transition aluminas are prepared by heating boehmite in a tube furnace 

under N~, and their surfa~g area de~mined with a Quantachrome surface 

area analyzer. Through U'Rb and - =Cs solid state nmr, the following 

questions: how will going from higher to lower surface areas affect the 

relative formations of the salt and surface species, and how will the 

varying forms of the alumina affect the motion of the cations on the 

surface, will be addressed. This work was partially supported by the 

National Science Foundation, grant #CHE86-I1306. 

i. Cheng, J. T. and Ellis P. D., submitted to J. Amer. Chem. Soc.

178 CROSS-POLARIZATION NAS NMR OF 27AI IN =- AND T-ALUMINA. 

H. Douglas Morris and Paul D. Ellis 



Columbia , South Carolina 29208 

The NMR characterization of catalyst supports such as T- and ~- 

aluminas has been accomplished through the observation of "probe" 

molecules absorbed on the surface. This methodology is accurate only for 

the sites and site distributions accessible to the probe, we report here 

intrinsic observation of surface A1 sites on ~- and y- alumina via 

~I CPMAS.- The absence of sub-surface IH allows only surface Br~nsted 

site A1 atoms to contribute to the spectra. This observation combined 

with cross-polarization to quadrapolar nuclei will allow the surface 

characteriza-tion of many catalytic supports which hitherto were 

described via probe molecules. 

We have been able to clearly distinguish octahedral from tetrahedral 

A1 sites. These sites have shown a population distribution dependent on 

the degree of surface dehydration. The addition of a weak Lewis base, 

pyridine, has shown selective signal enhancement of the T site over the 

O h site, which agrees with Majors a~d Ellis, in the a~signment of a 

hYgher percentage of T d Lewis sites. 

Experimental spectra are presented for different levels of surface 

dehydration, and addition of pyridine. Analysis of T I and T b~havior 

is presented to describe the spin-dynamics of the surface ;AI-IH 

interaction. This work was partially supported by the NSF, grant #CHE86- 

11306. 

i. Ellis, P. D. and Morris, H. Douglas, submitted to J. Am. Chem. Soc. 

2. Majors, P. D. and Ellis, P. D., J. A. C. S., 109, 1648 (1987). 

179 I 

DYNAMICS OF CHAIN SEGMENTS IN THERMOSKT RESINS* C. G. Fry and 

A. C. Lind, McDonnell Douglas Research Laboratories, P. O. Box 516, 

St. Louis, Missouri, 631 66 

The dynamics of chain segments between crosslinks in thermoset 

resins are investigated by use of solid-state deuterium NMR and 

molecular modeling techniques. Diamino-alkanes labeled at specific 

sites are used as curing agents for the thermoset resins. ~H NMR 

spectra obtained at various temperatures are sensitive to the site- 

specific motions of the alkane chain. Molecular modeling provides a 

powerful technique for interpreting the NMR spectra, and forms a basis 

for the modeling of crosslinked polymers in general. The effects of the 

mobility of the crosslink points at the chain ends, of the alkane chain 

length, and of intermolecular chain interactions on the line shapes will 

be discussed. 

*This research was conducted under the McDonnell Douglas Independent 

Research and Development program. 

188

. o 

. o 

180 l17o/Is NMR MICROSCOPY AT CWRU: G. Mateescu* G. Yvars D. Pazara and 

N.A. Alldridge b Departments of Chemistry and Biology b Case Western Reserve University 

Cleveland, Ohio 44106. 

A 9.4 T NMR microscope recently installed on our MSL-400 is opening fascinating new 

avenues for interdisciplinary research on our campus. The outstanding feature of the 

system is a double resonance probe which allows exact superposition of 170 and IH 

images taken from the same slice of the specimen. This is particularly useful in 

human, plant, animal, or materials studies where 170 is used either as direct imaging 

IH Microimage of 

African violet 

petiole; individual 

cells can be seen. 

IH image of 5 mm 

tube with H2170 

in 20 mm H2160 tube; 

note 0-17 

induced contrast. 

source or as a relaxation agent for characteristic enhancement of proton images. We 

will present the first results of combined 170/IH imaging which lead to new insights 

into the chemistry of life processes in plants and animals. The resolution limits will 

be illustrated with micrographs of human hair, plant, and animal cells and tissues. 

Imaging of chemical reactions and tridimensional diffusion will also be demonstrated. 

Support from NIH, NSF, and the Ohio Board of Regents is gratefully acknowledged. 

181 I APPLICATION OF I-D AND 2-D SODIUM-23 MAGNETIZATION 

TRANSFER NMR TO STUDY TRANSMEMBRANE CATION EXCHANGE 

Dikoma C. Shungu*and Richard W. Briggs 

Department of Radiology, 

University of Florida, Gainesville, FL 32610. 

While I-D magnetization transfer NMR experiments (i) are use- 

ful for determining kinetic rate information in the slow exchange 

regime, their use in the study of rapidly relaxing nuclei (e.g., 

Na-23) is a challenging practical problem due to difficulties in 

obtaining frequency-selective pulses which are short enough to en- 

sure negligible relaxation during their application. This poster 

describes how selective inversion of Na-23 resonances with a 

spin-lattice relaxation time as short as 12 msec can be effective- 

ly achieved. Na-23 inversion transfer experiments performed using 

this method are shown to yield reliable rate constants for ion ex- 

change across prototype lipid membranes. It is also shown that 2-D 

Na-23 NMR can be used to detect transmembrane cation exchange 

processes. Possibility of application to in vivo systems is dis- 

cussed. 

(i) S. Forsen and R.A. Hoffman, J. Chem. Phys., 3_99, 2892 (1963); 

40, 1189 (1964); 45, 2049 (1966). 

189

-- 182 I 

SUPPRESSION OF ARTIFACTS 

IN MULTIPLE ECHO NUCLEAR MAGNETIC RESONANCE 

G.J.Barker*, T.H.Mareci. 

Department of Radiology, 


Many techniques in both Magnetic Resonance Imaging (MRI) and 

Magnetic Resonance Spectrosopy (MRS) use two or more rf pulses to ex- 

cite the spin system and detect the echo signals which form between or 

after the pulses. After the initial excitation the evolution of the 

spin system depends upon relaxation times, exchange rates, diffusion 

constants and other properties, with the dominant mechanisms being 

determined by the details of the timing and tip angles of the pulses. 

In general many different echoes form during each acquisition inter- 

val, one of which carries the information required. The others lead to 

distortion of peak heights and line shapes in MRS, and to ghost images 

and similar artifacts in MRI. 

The 'coherence transfer pathway' formalism (1) allows the evo- 

lution of each echo to be studied and suggests methods of removing the 

unwanted signals. Phase cycling schemes haye been investigated which 

cause cancellation of the unwanted echoes, in certain cases during a~l 

acquisition intervals of a multiple echo sequence. Such schemes re ~ 

qulre a large number of transients to be collected, however, so a 

second method has been developed whereby the systematic application of 

magnetic field gradients produce similar results within a single tran- 

sient. Examples of the a~plication of both methods to the spin echo 

and TART (2) sequences In Imaglng, and to RED NOES¥ (3) in spectros = 

copy, show their success in remove artifacts. 

This research was supported in part by NIH Biotechnology 

Resource Grant (P41-RR-02278) and the Veteran Administration 

Medical Research Service. 

(1) G.Bodenhausen et al. , J. Magn. Reson. 58, 370, (1984) 

(2) T.H.Mareci et al. , J. Magn. Reson. 67, 55, (1986) 

(3) T.H.Mareci et a]. : 27th RNC_ R~]t~mn~A (lqR~% 

--183 I 

QUANTITATION OF EXCHANGE RATES 

USING THE RED NOESY SEQUENCE 

M.D. Cockman* and T.H. Mareci 

Departments of Chemistry, Radiology, and Physics 


We have previously introduced the RED NOESY pulse sequence 

for the simultaneous acquisition of several 2D NOESY spectra, each 

with a different mixing time (i). The RED NOESY sequence is similar 

to the NOESY sequence but the final 90 degree pulse of the latter is 

replaced by a series of "read" pulses of tip angles less than 90 de- 

grees to sample the exchanging longitudinal magnetization. This is 

the same principle behind the TART and STEAM T1 imaging sequences 

(2,3). Recently, Meyerhoff, et.al, have applied the sequence to a 

small lactone and report good success in routlne use of the pulse se- 

quence for the observation of NOEs (4). We have investigated the use 

of RED NOESY for the quantitation of exchange rates for three small 

N,N-dimeth[lamides. The most limiting aspects of RED NOESY are: i) 

that the slgnal acquisition time imposes a lower bound on the mixing 

times and 2) that the read pulses form unwanted echoes. We present a 

homospoiling scheme designed to overcome the second factor and exam- 

ine the implications of the first. 

This research was supported in part by the NIH Biotechnology 

Resource Grant (P41-RR-02278) and the Veterans Administration Medical 

Research Service. 

(I) T.H. Mareci, S. Donstrup, and M.D. Cockman, 27th ENC, Baltimore, 

1986. 

(2) T.H. Mareci, W. Sattin, K.N. Scott, and A. Bax, J. Magn. Reson, 

67, 55 (1986). 

(3) A. Haase and J. Frahm, J. Magn. Reson. 65, 481 (1986). 

(4) D.J. Meyerhoff, R. Nunlist, and J.F. O'Connell, Magn. Reson. 

Chem., 843, Oct (1987). 

190

To be presented at the 29th Experimental Nuclear Magnetic Resonance Spectroscop~ 

Conference, April I?-21, 1988 at Rochester, New York. 

1 84 I MULTINUCLEAR N-MR METHODOLOGY FOR DECONVOLUTING NATURAL 

MIXTURES AND CATALYTICALLY ACTIVE LAYER SILICATESt: Arthur R. Thompson*, 

Kathleen A. Carrado and Robert E. Botto, Chemistry Division, Argonne National 

Laboratory, 9700 South Cass Avenue, Argonne, IL 60439 

The combined use of a variety of pulse sequences and variable field has expanded 

the utility of solid-state aluminum-27 and silicon-29 NMR of layer silicates. 

The goal of this research has been to improve our knowledge of the possible roles 

of layer silicates in coal formation and catalysis. Many natural systems such as 

coal contain a mixture of layer silicates and their similar structures coupled 

with a lack of uniformity within a clay often yield broad overlapping spectra. 

Therefore, we analyzed several clays and their chemically modified variants to 

determine how to selectively distinguish that particular layer silicate. Some 

layer silicates when chemically modified to increase their catalytic activity 

show radical changes in their NMR spectra while others show remarkably little 

change. We have used these selective methods to determine which layer silicates 

present are more intimately associated with the organic portion of coal, and 

hence more likely to have played a role in coaliflcati0n. We feel these results 

demonstrate the feasibility of using NMR spectroscopy to study complex systems of 

layer silicates. 

tWork performed under the auspices 

Division of Chemical Sciences, U. 

number W-31-109-ENG-38. 

of the Office of Basic Energy Sciences, 

S. Department of Energy, under contract 

PARSING THE EDITED 1H NMR SIGNALS INTOI2c-1H ANDI3C-IH SUBSPECYRA: 

185 I ASTRATEGYTO STUDY SPECIFIC A£TIVITY IN VIVO. 

T. Jue* 

Dept. Molecular Biophysics and Biochemistry, Yale University, ~wHaven, Ct. 06511 

The general concern with the indirect detection experiment is sensitivity 

enhancement; a particular requirement of an in vivD experiment is specific activity. 

Tracing the metabolic flux entails an isotopic precursor infusion and a subsequent 

product analysis. However, the product is diluted by fluxes through the many path- 

ways, start'.~ng with endogenous, unlabeled precursors. 

With 13C isotope strategy both the 12C-IH and 13C-I~ si~%als are neoessary 

to access fractional enrichment information. St~m~dard [ C[-'H heteronuclear 

editing sequence (i) does not always yield the 12C-IH signal, being often masked 

by the background lipid reson~ces. Howe~. homonuclear editing sequences will 

select sinultaneously the 12C- H and 13C- H resonances (2). 

Because in vivo experiments are conducted at lower field, ~e have refined 

the editing strategy to separate the edited 12C-IH and 13C-IH signals into sub- 

spectra. This strategy permits us to decouple and to impl~t the fractional 

.enrichment study at lower field. 

i. M. R. Bendall, D. T. Pegg, D. M. Doddrell, and J. Field J. Am. Qhem. Soc. 103, 

934, 1981.; R. Freeman, T. H. ~reci, G. A. Morris J. Magn. Neson. 42, 341, 1981. 

2. T. Jue J. Magn. Reson. 73, 524, 1987. 

191

186 (Poster) 

The 13C Relaxation Behavior of Ethane Through Its Critical Point 

Ronald F. Evilia and Scott L. WhittenSurg:' Dept. of Chemistry, 

Univ. of New Orleans, New Orleans, La. 70148 

, Jan M. Robert: Dept. of Chemistry, S.G. Mudd Bldg. #6, Lehigh 

Univ., Bethlehem, Pa. 18015 

The longitudinal relaxation time of 13C in the ethane molecule has been 

measured over a temperature range of -i01 to +50°C, for a sample at the 

critical density. T I appears to vary with temperature, as anticipated; 

however, a discontinuity in the relaxation behavior is apparent at the 

critical point. From the experimental data, the critical constant may 

be obtained. 

[~ 1 87 INMR INVESTIGATION OF THE CYCLOPHILIN:CYCLOSPORIN COMPLEX. Heald SL, 

Gooley P, Armitage IM, Johnson C, Harding MW*, Handschumacher RE*. Departments of 

Molecular Biophysics and Biochemistry, Diagnostic Radiology and *Pharmacology, Yale 

University Schoor of Medicine, New Haven, CT 06510. 

Cyclophllln (CyP) is a low molecular weight protein which specifically binds 

the potent immunosuppressant, cyclosporin A (CsA). The amino acid sequence has been 

determined (163 residues, Mr 17,737) on the major bovine isoform of CyP. The primary 

goal of this work is to identify the CsA-binding site in cyclophilin. This 

investigation has proceeded along 3 pathways: (I) conformational studies on the 

drug, CsA; (II) probing the CsA:CyP complex by IH NMR and (III) through NMR-labelled 

CsA analogues. 

Cyclosporln A goes from a single averaged conformation observed in CDCI 3 to 

multiple conformations in polar solvents. Several of the individual conformations 

observed in the CH3OD/"H20 mixture are identified based on the HOHAHA and ROESY spin- 

locking experiments. 

Drug-free cyclophilin has been characterized by the IH 2D NMR experiments: 

COSY, HOHAHA and NOESY. Amino acid types have been assigned in the aromatic and 

upfield methyl spectral regions. A comparative study has been carried out on the 

CsA:CyP complex. The amino acid residues predominately involved in complexation are 

readily identified by this method. Site-specific assignment of these residues is 

assisted by the use of NMR-labelled CsA analogues in conjunction with heteronuclear 

multiple quantum and isotope-directed nOe NMR experiments. (Supported by NIH grant 

DE 18778, American Cancer Society CH-67-28 and Merck & Co., Inc.). 

192

INHIBITION OF ALANINE RACEMASE BY THE PHOSHATE ANALOG OF 

188 ~LANINE, I-(AMINOETHYL)PHOSPHATE (ALA-P): IDENTIFICATION 

~ A SCHIFF BASE LINKAGE IN THE ENZYME-INHIBITOR COMPLEX BY SOLID STATE 

-N-NMR. , 

Val~rie Copi~, W. Stephen Faraci, Christopher T. Walsh, 

and Robert G. Griffin 

Departments of Chemistry and Biology, 

and the Francis Bitter National Magnet Laboratory, 

Massachusetts Institute of Technology, Cambridge, MA 02139 

Alanine racemases are a group of pyridoxal-5'-phosphate (PLP) 

containing enzymes which catalyze the racemization of L- and D-alanine, 

the latter being an essential component of the peptidoglycan layer of 

bacterial cell wall. Although the kinetics of inactivation of alanine 

racemases from gram positive bacteria by Ala-P have been well 

determined, the structure of the inactive enzyme complex remained to be 

determined. 

Solid State NMR technique was used to address the issue of whether 

or not AIa-P forms a covalent linkage to ~e enzyme's PLP cofactor. 

Solid State, Magic Angle Sample Spinning N-NMR experiments combined 

with cross-polarization technique were performed at low temperatures on 

microcrystals of Ala-P-alanine racemase complex. The NMR results show 

that the inactive complex forms a protonated Schiff base to 

pyridoxal-5'-phosphate (PLP) in the enzyme's active site. Solid State 

NMR spectra of Schiff bases and Ala-Pl~Odel compounds were also 

accumulated to provide a database of N-chemical shifts. 

Dynamic and Confromational Structure of CORD Factor Glycolipids in 

] 8 9 I Model Membranes as Determined by Solid-State 2H NMR: 

, r 

R. A. Byrd and T. K. Lira, Biophysics Laboratory, Division of Biochemistry and 

Biophysics/FDA, 8800 Rockville Pike, Bethesda, MD 20892 

As part of our studies of cell surface carbohydrates and their intermolecular interactions, 

a recent study has dealt With the structural features of a particular glycolipid. Our studies are 

aimed at elucidating the role of these glycolipids in defining the physical and chemical properties 

of the mycobacterial cell surface. The glycolipid is a synthetic analog of a natural component 

referred to as CORD FACTOR. Certain virulent strains of bacteria form long filaments or 

serpentine-like 'cords'. The cord factor has been isolated and characterized as trehalose-6,6'- 

dimycolate. Recently, there is renewed interest in its immunostimulant properties and its 

antitumor activities, which prompted the testing of several synthetic analogues. 

The dynamical behaviors of the trehalose head-group and of the hydrocarbon tails 

(dipalmitate and di{2-tetradecylhexadecanoate}) in the liquid-crystalline phase were investigated 

by solid-state 2H NMR. Selective synthetic incorporation of 2H on both saccharide rings and the 

hydrocarbon chains leads to a complete study of the entire molecule. From the fully assigned 2H 

spectra and the respective quadrupole splittings, the conformation of the head group was 

determined in a number of systems. Clear evidence exists for pronounced ring strain in the 

trehalose moiety. This may have significant implications for understanding the surface 

carbohydrate structures such as LPS. 

193

THE VISUALIZATION OF PROBE ELECTRIC FIELDS 

by 

190 j D.I. Hoult* and C-N. Chen 

Biomedical Engineering and Instrumentation Branch, Division of Research Services, 

Bldg. 13, Rm. 3W13, National Institutes of Health, Bethesda, MD 20892. 

Conservative electric fields in the sample volume of NMR probes are responsible for twin 

evils - the detuning of the probe upon insertion of a sample with high dielectric constant (e.g. 

tissue or water, E = 80), and losses which result in sample heating and reduced signal-to-noise 

ratio. Several probe designs have adopted the strategy of distributing the tuning capacitance 

about the probe coil in order to reduce the electric fields and extend the usable frequency range, 

but it is always difficult to know whether or not the adopted strategy has been successful, the 

principal difficulty's being in distinguishing" dielectric" loss from "magnetic" (induction) loss. 

Differentiation of these two mechanisms usually requires a tedious plot of loss versus 

frequency, the onset of dominant dielectric loss being the point at which losses increase far more 

rapidly than the usual = (02 dependency. 

Working with a simple method first described by Chute and Vermeulen t, we have been able 

to produce cheaply and quickly a color picture of the electric fields in a probe - an inestimable 

aid in deciding whether a design is viable. The required components are a sheet of resistive paper 

glued to mylar film containing temperature-sensitive liquid crystals. The combination is then 

mounted as necessary to simulate the sample, and when power is applied to the probe, that 

portion of the sheet that is in a sizable electric field is warmed, whereupon the crystals change 

color. Clearly, contours of constant color deliniate regions of constant electric field, and 

undesirable "hot spots" are quickly noticed. Thus the poster will give fabrication details, and 

results from several common coil configurations will be displayed. 

IF. S. Chute and F. E. Vermeulen, AJP 42, 1075-1077, 1974. 

191 ] NMR ANALYSIS AND IMAGING OF OIL CORES: W. A. Edelstein .1, 

H. J. Vinegar 2, P. B. Roemer 1, P. N. Tutunjian 2, and O. M. Mueller 1. (1) GE Corporate Research and 

Development Center, Schenectady, NY 12345. (2) Shell Development Company, Houston, TX 77025. 

Oil cores in the form of cylinders up to 6" diameter are routinely taken during oil exploration and 

production. It is important to measure several petrophysical properties of the oil cores, such as oil and 

water saturation, porosity and permeability. Traditional methods of obtaining such information involve hot 

solvent extraction and take several days or longer. NMR can, in many cases, make the required 

measurements in minutes. Imaging allows variations of the rock and fluid properties to be visualized on 

the scale of mm and allows discrimination against artefacts such as fractures and invasion of the core by 

drilling mud. There are a number of technical difficulties involving the NMR. In certain rock formations, 

such as clean sandstones and carbonates, the NMR linewidth is narrow and the oil and water saturation 

can be easily separated by chemical shift spectroscopy or imaging. In other cases, such as shaly 

formations, the water and oil linewidths may be inhomogeneously broadened. NMR imaging under these 

circumstances requires fast and strong magnetic field gradients. We have shown that the NMR signals in 

some of the shaly sandstones can be refocussed and should be imageable with very fast data acquisition. 

We are presently examining the relaxation mechanism in sandstones by comparative proton/deuterium 

studies, and are investigating the suitability of other nuclei (i.e. carbon and sodium) for 

measurementftmaging of core properties. 

194

192 RESOLUTION ENHANCEMENT OF PHOSPHORUS-31 SPECTRA 

I 

THE USE OF CDTA IN PERCHLORIC ACID EXTRACTS OF DICTYOSTELIUM DISCOIDEUM 

Kenneth L. Williamson* and Ethel F. Fromm* 

Department of Chemistry, Mount Holyoke College, South Hadley, MA 01075 

Dramatic increases in resolution of 31p spectra have been found in 

perchloric acid extracts of the cellular slime mold, Dictyostelium discoideum, 

by using CDTA (trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid 

hydrate) in place of the traditional EDTA (ethylenediaminetetraacetic acid) to 

L 193 

complex with cations. These high resolution spectra have been used to study 

the phosphorus metabolism of D, discoideum during all stages of its 

development during the 24 hr time period in which it undergoes, under 

conditions of starvation, development from single-celled amoebae to a 

multicellular organism containing stalk cells and spores. The present study 

has focused on the latter part of the developmental process. 

IADDITIVITY OF CARBON-13 SPIN-LATTICE RELAXATION TIMES IN OCTENES 

Kenneth L. Williamson*, Maureen A. Simonds* and Thomas R. Stengle 

*Department of Chemistry, Mount Holyoke College, South Hadley, MA 01075 

Department of Chemistry, University of Massachusetts, Amherst, MA 01003. 

Carbon-13 spin lattice relaxation times have been measured for a number of 

isomeric octenes in order to explore the relationships between T I and 

molecular dynamics and conformations. Systematic trends were observed in the 

relaxation times so that an empirical relationship could be derived which 

allows one to estimate the T I of a given carbon atom by summing additivity 

parameters based on the location of the given carbon relative to the double 

bond, to methyl groups, and to centers of branching. These additivity 

parameters were obtained by performing a linear multiple regression analysis 

on the Tl'S of individual carbons in the octenes. The T I of a given carbon 

atom can then be derived by simply summing appropriate combinations of 

regression coefficients in exactly the same way that 13C chemical shifts can 

be calculated. 

195

--194 

I CPMAS ANALYSIS OF A POLYIMIDE/GLASS CIRCUIT BOARD: 

B. L. Myers-Acosta*, S. J . Selover, Lockheed Missiles & Space Company, 

Inc., Sunnyvale, California 94088-3504. 

The effects of starting material chemistry and processing on the final 

properties of cured polyimide/glass composites has been investigated 

using CPMAS spectroscopy. We have found that both changes in 

stoichiometry and processing can be detected using this technique. 

Previously, only starting material chemistry could be readily 

investigated making it difficult or impossible to evaluate the effects 

of processing on the material chemistry. We have found that several 

features of the performance of these polyimide materials, after 

processing into circuit boards, are a function of the interaction 

between material chemistry and processing. CPMAS spectroscopy 

provided a unique way to evaluate the chemistry of the cured composite 

in finished parts to establish the processing requirements of specific 

materials. Further, processing latitude could be evaluated by 

examining the chemical state in cured composites from various 

lamination schedules. Spectroscopic details will be presented. 

--195 I A STUDY ON 3',5'-AMP BY TWO-DIMENSIONAL DOUBLE QUANTUM 

SPECTROSCOPY IN 'H NMR, Gang Wu*, Wei Gun, Y. Huang, Shouping Jiang, Shaohui LJan, 

Physics Department, East China Normal University, Shanghai 200062, People's 

Repub]ic of China. 

The results of two-dimensional double quantum spectroscopy on 3',5'-AMP will be 

presented. The resonances of H(2) and H(8) are resolved in the spectrum, which are 

partially overlapped in ttle 1D spectrum, and the coupling of H(1')-H(8) is revealed 

from which we are able to deduce that the glycosyl bond conformation of 3',5'-AMP 

in solution (ph 7, O.04M, 23°C) is in the form of syn conformation with the 

dihedral angle ~ in a range of 79 ° ~ 90 ° . The spectrum also shows 

the direct coupling between H(2) and H(8) by Type I signals, which coupling is 

unresnlvable in ID spectr.m because of its small value. 

c,., 

C,+ o~ 

¢8 

~o-P=o q'Hl~ H /1 It 

*Present address: Department of Chemistry, York University, 4700 

Keele St., North York, Ontario M3J 1P3 Canada. 

196

196 1 

TR FLUOROETHOXY DERIVATIVES: SELECTIVE DEACTIVATION OF 

OXYGEN CONTAINING FUNCTIONAL GROUPS IN LANTHANIDE INDUCED SHIFTS 

AND/OR RELAXATION NMR STUDIES. C. Wild*, C. Tsiao*, T. E. Glass, 

J. Roy, H. C. Dorn, Chem. Dept. VPI&SU, Blacksburg, VA 24061. 

During the last twenty years, a considerable number of 

lanthanide shift reagents (LSR) have been used for structural 

studies in organic chemistry. These shift reagents generally 

function as weak Lewis acids which can form weak complexes with 

nucleophilic functional groups present in the substrate of 

interest. For the case of polyfunctional molecules, most 

structural studies have been hampered because of the posssiblity 

of complexation at the various nucleophilic sites in a given 

molecule. 

To overcome this problem, we have made use of trifluoro- 

ethoxy group to selectively deactivate oxygen containing func- 

tional groups towards complexation with lanthanide shift 

reagents. Our initial studies illustrate the utility of these 

reagents by comparing the lanthanide induced shifts (LIS) of 

several trifluoroethyl ketals with their corresponding ethyl 

analogs. The practical aspects of these reagents are explored 

in a study which involved the selective deactivation of 

specific sites in several polyfunctional molecules. In this 

manner, structural information (e.g. cis/trans isomer assign- 

ments) can be obtained from the LIS and spin-lattice relaxation 

(TI) data. 

197 I TIME DOMAIN ENDOR STUDIES OF DISORDERED SOLIDS: P. J. Tindall, H. 

Bernardo, and H. Thomann, EXXON Corporate Research Laboratory, Route 22 East, 

Annandale, N. J. 08801 

Spectral simplification, resolution enhancement, and sensitivity enhancement are well 

known advantages of multiple frequency techniques used in NMR. The ability to 

coherently excite and coherently transfer longitudinal or transverse magnetization 

among sub-levels of the spin system elgenstates is fundamental for the success of 

most of these experiments and is only possible with time domain pulsed excitation. In 

contrast to NMR, the most widely applied multiple resonance technique in ESR, the 

ENDOR experiment, has traditionally been performed in the frequency domain. However, 

recent advances in instrumentation have now made time domain ENDOR more feasible. 

The time domain analog of the CW-ENDOR exper-lment [is magnetization transfer (MT) 

ENDOR using the Davies pulse sequence. MT-ENDOR has the advantage that the ENDOR 

enhancement does not depend on the ratio of the electron and nuclear T 1 rates as it 

does in CW-ENDOR. Furthermore, time domain excitation also makes possible more 

complex double resonance experiments which depend on coherence transfer, such as 

CT-ENDORand splnor ENDOR recently demonstrated by Mehring et al. The general 

applicability of these techniques to disordered solids will be governed by electron 

T 1 and T m (phase memory) times which are typically shortened by disorder effects. 

Fortunately, in many cases of interest, relaxation times for hydrocarbon radicals in 

condensed hydrocarbons are sufficiently long for successful magnetization and 

coherence transfer experiments even at room temperature. Experiments on transition 

metal ion complexes and metal clusters are possible at liquid He temperatures. Some 

recent time domain ENDOR results on isolated coal macerals, polyacetylene, and frozen 

solutions of transition metal ion complexes will be presented. 

197

198 I NUMERICAL STUDIES OF STIMULATED ESEEM WAVEFORMS: H. Jin and H. 

omann, Corporate Research Laboratory, EXXON Research and Engineering Company, 

Route 22 East, Annandale, N. J. 08801 

Electron spin echo envelope modulation (ESEEM) spectroscopy has proven to be a 

powerful method for studying hyperfine and quadrupolar interactions of nuclei 

coordinated to paramagnetic electron centers. Important areas of application 

include the study of nitrogen coordination in metalloproteins; surface adsorbate 

interactions of supported transition metals; and the electron density distribution 

on organic paramagnetic radicals important in photosynthesis and in photoexcited 

triplet states. Analysis of the ESEEM patterns for S-I/2, I -I spin systems in 

randomly oriented solids is usually performed using frequency spectrum analysis. 

ESEEM spectra are simulated by calculating the superposition of the two powder 

pattern quadrupolar spectra obtained when the isotropic hyperfine coupling adds or 

subtracts to the Zeeman field. Such simulations will accurately predict ESEEM 

frequencies but will usually not even give qualitatively correct modulation depths 

in the ESEEM waveform or reproduce the correct linewidths in the ESEEM spectrum. 

These depend on the anisotropic hyperfine interactions and are therefore important 

spectroscopic parameters which can reveal additional chemical information about the 

coordination complex. This provides the impetus for numerical studies of the ESEEM 

spectrum and time domain waveforms in which the psuedodipolar as well as the 

isotropic hyperfine and quadrupolar interactions are retained. Some preliminary 

numerical results of this study will be presented in this poster. In particular, we 

explore the importance of the relative magnitudes of the Zeeman, isotropic and 

psuedodipolar hyperfine, and quadrupolar interactions in determining the modulation 

depth of the ESEEM waveform. We also explore the ESEEM waveform and frequency 

spectrum in the presence of anisotropic hyperfine interactions with only a partial 

cancellation of the Zeeman field by the isotropic hyperfine coupling. 

-- 1 99 l HIGH PRESSURE 13C CROSS-POLARIZATION AND SPIN RELAXATION STUDY OF 

ADAMANTANE: K.O. Prins and D. van der Putten, Van der Waals Laboratory, University 

of Amsterdam, Postbus 20216, 1000 HE Amsterdam, The Netherlands. 

The poster presents a description of a double resonance probe suitable for IH-I~C 

cross-polarization experiments at hydrostatic pressure up to 10 kbar. The probe is 

placed in a liquid nitrogen cryostat, constructed inside the 13 cm bore of a 4.2 T 

superconducting magnet. 

Cross-polarization has been used in a study of the effect of high pressure on 

molecular reorientation in the orientationally disordered solid phase I and in the 

ordered phase II of adamantane. It is shown that knowledge of the iH and 13C 

relaxation times T and T allows distinction between isotropic rotational diffusion 

i 10 

and discrete reorientations in the two solid phases. In phase I adamantane spends 

a non-negligible time between its equilibrium orientations. In phase II the experimen- 

tal results are well described by a discrete reorientational model. A broadening of 

the 13C resonance observed while spin-locking the protons occurs at increasing 

pressure. 

198

200 

INTERPRETAT IION OF 13 C NHR MIXTURE SPECTRA BY MULTIVARIATE ANALYSIS: 

Trond Brekke, 01av M. Kvalheim and Einar Sletten 

Dep. of Chemistry, Univ. of Bergen 5007 Bergen, Norway 

High-resolution 13C NMR spectroscopy oT complex mixtures, e.g fossil hydro- 

carbons, provides large amounts of data. The interpretation and quanti- 

fication of such spectra require the use of multivariate data analysis. 

Principal Component (PC) analysis of 13C spectra of 12-component synthetic 

hydrocarbon mixtures £nd£cates that more than 98Z of the variat£on in the 

spectra is due to chemical variation among the Samples and an efficient 

means of reveaZing correZations among resonances (e.g. subspectra of single 

components) is presented. Partial-Least-Squares (PLS) regression is used to 

establish models for the prediction of densitY, mean molecular weight and 

refractive index of the samples from the spectra. 

2oi I 

THE CORRELATION OF IH-lmF COUPLINGS BY HETERONUCLEAR BODE _PULSED DECOUPLING 

(HUltPD) 

Stephen H. Grode and Russell W. Gillis, The Upjohn Co., Fine Chemicals, 

Kalamazoo, HI 49071 

The identification and characterization of fluorinated compounds is complicated 

by the ubiquitous nature of the 1H-19F scalar interaction. This is 

particularly true of fluorinated steroids in which the observation of 5 bond 

1H-19F couplings is not unusual. The typical method used to identify IH-19F 

coupling is to apply a CW signal to each proton of interest and observe its 

effect on the 19F resonance. This is unsatisfactory for three reasons: I) The 

small long range couplings often go unobserved, 2) In a crowded spectrum it is 

difficult to irradiate a single proton without affecting neighboring protons, 

and 3) If a number of protons need to be irradiated the experiment is time 

consuming. These problems can be alleviated by performing the experiment in 

the opposite configuration (i.e. 19F decouple IH observe in place of 1H 

decouple 19F observe). A HeteronUclear Bode -pulsed Decoupling (HUMPD) method 

was developed to acquire 19F spin decoupled 1H-NMR spectra. This is a gated 

decoupling method in which 19F transmitter is triggered to pulse between 

sampling times. The purchase of a heteronuclear decoupler is not required. 

This method is demonstrated in the ID and 2D (HUMPD-COSY) realms by application 

to fluocinolone acetonide. In the 2D experiment, HUMPD is applied during 

acquisition, thus collapsing the IH-IgF interaction during the T2 time domain 

only. This yields a 2D spectrum in which it is possible to observe all the 

IH-IH couplings, as in a normal COSY, and identify the fluorine interacting 

protons by virtue of a crosspeak collapse along F2. 

199

L 

202 ___] 

SOLID STATE BACK PROJECTION IMAGING 

JOHN LISTERUD AND GARY DROBNY 

DEPARTMENTS OF ELECTRICAL ENGINEERING AND CHEMISTRY 

UNIVERSITY OF WASHINGTON, SEATTLE, WA 98195 

Abstract 

The requirements of an NMR imaging system dedicated to materials science will be 

quite distinct from those of medical imaging. Not the least of these differences will be the 

degree of flexibility demanded of a research laboratory system as compared to the turn- 

key philosophy of the clinical imager. In particular, the materials sciences challenge the 

spectroscopist to combine the classic NMR spectroscopies with the imaging experiment. 

To these ends we describe the construction of a multi-purpose microscopic NMR imaging 

probe for use on a standard spectrometer, and the efficient adaptation of standard two 

dimensional NMR data processing utility to image processing. The probe is capable of 

a variety of experiments, including the Kumar-Welti- Ernst experiment, backprojection 

by mechanical rotation of the sample, and backprojection by electronic rotation of gradi- 

ents. Because of its simplicity, backprojection promises to be especially straightforward 

to combine with spectroscopic techniques such as chemical shift and multiple quantum 

spectroscopy. Furthermore, "macro" feature of the standard two dimensional NMR data 

processing utility has a natural extension to tailored image processing, as demonstrated 

here by Tl and diffusion weighting of image grey scales. 

2o3 I 

LONG-RANGE SHIELDING AND CHEMICAL SHIFT IN SILICON CARBIDE 

POLYTYPES. M. F. Richardson, J. S. Hartman*, and D. Guo, Department of 

Chemistry, Brock University, St. Catharines, Ontario L2S 3AI, Canada. 

Silicon carbide, which has many polytyplc modifications of a very simple and 

symmetric structure, is an excellent model system for exploring relationships 

between chemical shift and crystal structure in network solids. A simple 

McConnell equation treatment of bond anlsotropy effects (H. M. McConnell, J. 

Chem. Phys., 1957, 27, 226) predicts chemical shifts for s ilicon and carbon 

sites which agree well with experiment (J. S. Hartman et al ., J. Amer. Chem. 

Soc., 1987, 109, 6059), provided that contributions from bonds up to i00 A from 

the site are included in the calculation. The calculated shlf ts depend on both 

the layer stacking sequence (i.e., the polytype) and on the spacings between 

silicon and carbon layers. Unambiguous assignment of peaks to lattice sites 

should now be possible for all polytypes, but chemical shifts are so sensitive 

to layer spacings that our calculations are limited by the accuracy of layer 

spacing values determined by careful X-ray diffraction work. It appears that 

chemical shifts in network solids can in principle be more sensitive to atomic 

positions than the most carefully obtained X-ray data. While X-ray diffraction 

is necessary to determine the polytype, the most accurate values of layer 

spacings in polytypes and other highly correlated structures should in future be 

derived from nmr chemical shift values rather than from the X-ray data. 

200

204 RECENT PROGRESS IN HIGH RESOLUTION NMR OF SOLIDS. Charles 

E. Bronnimann, Stephen L. Dec, James S. Frye, Bruce L. 

Hawkins and Gary E. Maciel, Regional NMR Center, Colorado State 

University, Fort Collins, CO 80523 

Over the past several years this NSF-sponsored regional instrumentation facili- 

ty (303-491-6455) has developed and applied a number of experimental strategies in 

ongoing NMR studies of a variet~ of solids.loTe~niques used have included CP/MAS, 

very high speed (> 20 KHz) MAS, =H CRAMPS, =~F-~C cross polarization, magic-angle 

hopping and angle flipping; in each case the necessary instrumentation has been de- 

signed and developed in the laboratory. Classes of materials that have been studied 

include a variety of crystalline and amorphous organic and inorganic solids, poly- 

mers and polymer blends, catalytically important surface systems, materials impor- 

tant in separation science, organic goechemical solids, solid electrolytes, semi- 

conductors and superconductors. 

Current experimental thrusts in this laboratory include the improvement of 1H 

CRAMPS characteristics, time-domain CRAMPS experiments, use of higher magnetic 

fields (11.7 and 14.0 T) and higher MAS rates (> 23 kHz), development of new pulse 

sequences, use of multiple-quantum techniques for examining hydrogen clustering, 

improving pulse programming capabilities, and the integration and networking of 

modern and more powerful computer capabilities with our spectrometers. 

Selected examples of recent developments in these areas will be presented and 

discussed. 

205 

HIGH-FIELD PULSED GRADIENTDIFFUSIONMEAS~S 

Ronald L. Haner and Thomas Schleich 

Department of Chemistry, University of California 

Santa Cruz, CA 95064 

Self-diffusion measurements obtained by the use of pulsed gradient spin echo 

(PGSE) techniques are usually performed with modified spectrometers containing 

resistive magnets at static fields of 2.35 Tesla or less. Few measurements have 

been reported using spectrometers with superconducting magnets, and all have been 

done with relatively weak gradient strengths. We have developed pulsed gradient 

diffusion instrumentation for use in high field (7.05 Tesla) spectrometer systems, 

employing gradient strengths that have been tested up to I00 gauss/cm. 

The apparatus includes specially designed gradient probes and a simple, 

stable current pulser. The gradient coil fringe field is minimized by using an 

active screen, similar in design to that proposed by Mansfield and Chapman (J__~. 

Phys. E: Sci. Instrum. t 19, 540, 1986). 

Our PGSE spectrometer has been used to measure protein and solvent diffusion 

in protein solutions and i__nn vitro intact cellular systems. Lysozyme 

self-diffusion has been measured to an accuracy and precision of 5-10% in aqueous 

solutions at concentrations as low as 0.5% w/w. Solvent (H20 and }[DO) 

self-diffusion coefficients have been measured to an accuracy and precision of 

less than 3%. Extensions to studies of restricted and anisotropic diffusion, 

other nuclei, and spatially localized applications are anticipated. 

The description of this high field PGSE spectrometer system, experimental 

protocol, and some experimental results will be presented. (Supported by NIH 

grant EY 04033.) 

201

- - 206 

THE WORLD AND WONDERS OF 3H NMR SPECTROSCOPY: Philip G. 

/i.lliam:s. ,* National Tritium Labeling Facility, Lawrence Berkeley Laboratory 75-123, 

mverslty of California, Berkeley, California 94720. 

The NTLF is a national User Facility, funded by the National Institutes of Health. The Facility combines 

e availability of high levels of carrier free tritium gas, extensive radiochemical purification resources, and an 

n-house NMR instrument dedicated to tritium NMR spectroscopy. The NTLF combines its User service 

unction with core and collaborative research based on the use of hydrogen isotopes. 

Tritium is an excellent nucleus for NMR observation, but NMR applications in the chemical and biological 

ciences have been very limited in number. "Onepulse" tritium measurements can quickly and cleanly give the 

hemical shift and relative abundance of tritons in a sample, and in combination with other physical methods 

an rapidly assure quality control in labelling experiments. In catalysis hydrogen isotope exchange is readily 

nonitored, with the relative incorporation at each position of a substrate yielding specificity rules for the 

atalyst as well as mechanistic detail. 

Hydrogenation and halogen replacement reactions are the cornerstone of high level tritium labelling 

procedures. Little is known about concomitant side-reactions, but these are extremely important when specific 

abelling is required. Observation of tritium NMR peaks from supposedly "unlabelled" positions obviates 

hese extra mechanisms, and allows the choice of appropriate precursors and reaction conditions for the 

lesired tritiation. 

As one example, allylic methyl exchange in the hydrogenation of I]-methyl styrene to yield n- 

,ropylbenzene is readily detected, and the full range of isotopomers can be distinguished by J-resolved 

pectroscopy. Secondly, tritio-dehalogenation of 2-chloro-2'-deoxyadenosine with pure T2 does not give 

,roduct with the theoretical specific activity, and factors influencing this "dilution" may be followed. 

Important and developing uses of tritium NMR spectroscopy include monitoring of the conversion of 

ntermediates in biological systems, studies of substrate binding, and as an aid in spectral elucidation of proton 

~VMR spectra. The use of modern multipulse techniques in concert with simple and elegant older sequences 

aas the potential for giving a great deal of conformational and coupling information, through the interaction of 

I-H and 1-H atoms. NMR work at the Tritium Facility is intent on establishing the benefits and problems 

tssociated with tritium NMR spectroscopy of many diverse substrates - from simple organics to solids and 

nacromolecules. 

202

Page No. 

ACEVEDO, H F 165 

ACKERMAN, J J H 104 

ACKERMAN, J L 155 

ACKERMAN, J L 53 

ADAMY, S 175 

ALBRIGHT, M J 126 

ALDERMAN, D W 141 



ALLDRIDGE, N A 189 

ALLEN, L 28 

ALTOBELLI, S A 184 

ANDERSEN, N H 155 

ANDERSEN, N H 169 

ANDERSON, M E 166 

ARAJAN, S 139 

ARMITAGE, I M 192 

ARNOLD, B R 125 

ARORA, S 177 

ARUS, C 166 

ASHCROFT, J 121 

ASHIDA, J 113 

AVRAM, H E 152 

BACHOVCHIN, W H 38 

BAIN, A D 108 

BAIN, A D 127 

BALASUBRAMANIAM, S 139 

BANK, J F 143 

BANK, S 143 

BARBARA, T M 157 

BARKER, G J 190 

BARNES, R G 150 

BASTI, M M 176 

BAX, A 178 

BAX, A 36 

BAX, A 164 

BAZZO, R 137 

BECK, B 153 

BECKER, N N 104 

BEGEMANN, J 152 

BEHLING, R W 61 

BEHLING, R W 161 

BELL, R F 45 

BERNARDO, M 197 

BIELECKI, T 38 

BILDSOE, H 123 

BISHOP, K D 146 

BLUMICH, B 101 

BODENHAUSEN, G 32 

BOEHMER, J P 184 

BOHLEN, J -M 32 

BOLTON, P H 175 

BORAH, B 131 

BORDIA, R K 129 

BORER, P 144 

BORER, P 145 

BORER, P 143 

BORER, P N 146 

BORK, V 130 

BORNEMANN, V 162 

203 

BOTHNER-BY, A A 

BOTHNER-BY, A A 

BOTTO, R E 

BOTTO, R E 

BOUCHARD, D A 

BOUDREAU, E 

BOYD, J 

BOYER, R D 

BRANDOLINI, A J 

BRAUER, M 

BREKKE, T 

BRENNEMAN, M T 

BRENNEMAN, M T 

BRENNERT, G F 

BREY, W S 

BRIGGS, R W 

BRONNIMANN, C E 

BRONNIMANN, C E 

BROOKER, H R 

BROWN, S C 

BROWN, T R 

BROWN, T R 

BRUSCHWEILER, R 

BRYAN, R N 

BRYANT, R G 

BUCHANAN, G W 

BURNETT, L J 

BURUM, D P 

BUSHWELLER, C H 

BYRD, R A 

CABASSO, I 

CARDUNER, K R 

CARPER, W R 

CARRADO, K A 

CARVLIN, M 

CASTELLINO, S 

CASTELLINO, S 

CAU, F 

CAULEY, B J 

CAVA, R J 

CAYLEY, S C 

CERDAN, S 

CHACKO, V P 

CHARI, M 

CHEN, C-N 

CHESNICK, A S 

CHINN, M 

CHOBANIAN, M 

CHU, S 

COCKMAN, M D 

COFFIN, D B 

COLE, H B R 

COLLINS, M J 

CONWELL, E M 

COPIE, V 

CORY, D G 

COWBURN, D 

COZINE, M 

CREUZET, F 

CROCKETT, B 

Page No. 

165 

183 

98 

191 

161 

143 

137 

124 

171 

183 

199 

182 

182 

45 

109 

189 

20 

201 

153 

135 

124 

123 

35 

111 

149 

98 

114 

105 

125 

193 

103 

104 

105 

191 

139 

137 

136 

172 

138 

45 

165 

55 

129 

177 

194 

162 

185 

166 

132 

190 

105 

180 

134 

109 

193 

50 

121 

185 

24 

187

CROOKS, L E 

CROSS, T A 

CROSS, T A 

CROWTHER, M 

CROWTHER, M W 

CURTIS, J 

D'AVIGNON, D A 

DADOK, J 

DADOK, J 

DANDO, N R 

DARBA, P 

DARBA, P 

DAVIES, P K 

DEC, S F 

DEC, S L 

DELAGLIO, F 

DELAGLIO, F 

DELAGLIO, F 

DELAGLIO, F 

DELSUC, M 

DORN, H C 

DORN, H C 

DOUGHTY, D A 

DROBNY, G 

DUPREE, R 

DWYER, T J 

EARLY, T A 

EATON, H L 

ECKERT, H 

EDELSTEIN, W A 

EDELSTEIN, W A 

EDLUND, U 

EDMONDSON, D E 

EGGENBERGER, U 

ELLINGSON, W A 

ELLIS, P D 

ELLIS, P D 

ELLIS, P D 

ELLIS, P D 

ENRIQUEZ, R G 

EPSTEIN, W W 

ERNST, R R 

ESPINOSA, G P 

EUGSTER, A 

EVERS, A S 

EVILIA, R F 

EWY, C S 

FACELLI, J C 

FACELLI, J C 

FANG, 

FARACI~ W S 

FARNAN, I 

FARNETH, W E 

FEJZO, J 

FERRANTELLO, L M 

FINEMAN, M A 

FINEMAN, M A 

FITZSIMMONS, J R 

FORD, J J 

FOXALL, D 

Page No. 

152 

182 

182 

152 

103 

141 

103 

183 

165 

160 

167 

168 

173 

20 

201 

152 

145 

100 

146 

144 

28 

197 

157 

200 

179 

106 

126 

155 

159 

57 

194 

145 

108 

32 

53 

143 

187 

188 

187 

180 

140 

35 

45 

117 

103 

192 

104 

125 

149 

142 

193 

179 

129 

167 

112 

114 

110 

153 

111 

183 

204 

FOXALL, D 

FREDERICK, A F 

FREEMAN, D M 

FREEMAN, R 

FROMM, E F 

FRUEHAN, P 

FRY, C G 

FRYE, J S 

FU, JM 

FUJIWARA, T 

FUKUSHIMA, E 

GALVIN, M E 

GAO, X 

GARBETT, S P 

GARBOW, J R 

GARRIDO, L 

GARROWAY, A N 

GARROWAY, A N 

GARROWAY, A N 

GARROWAY, A N 

GERASIMOWICZ, W V 

GERSTENBLITH, G 

GESMAR, H 

GIAMMATTEO, P j 

GILES, R H 

GILLIS, R W 

GITTI, R 

GIVLER, R C 

GLASS, T E 

GLASS, T E 

GLICKSON, J D 

GLIMCHER~ M J 

GLOVER, H 

GMEINER, W H 

GONEN, 0 

GOOLEY, P R 

GORENSTEIN, D G 

GRAHN, H 

GRAHN, H 

GRAHN, H 

GRANDINETTI, P j 

GRANT, D M 

GRANT, D M 

GRANT, D M 

GRANT, D M 

GRANT, D M 

GRANT, D M 

GRANT, D M 

GREIG, R 

GRIESINGER, C 

GRIFFIN, R G 

GRIFFIN, R G 

GRIFFIN, R G 

GRIFFIN, R G 

GRODE, S H 

GRUNDY, H D 

GUIDOTTI, A 

GULLION, T 

GULLION, T 

GULLION, T 

Page No. 

132 

128 

156 

42 

195 

135 

188 

201 

156 

115 

184 

69 

136 

133 

112 

53 

170 

49 

171 

170 

170 

129 

120 

175 

165 

199 

28 

184 

28 

197 

129 

155 

57 

174 

14 

192 

156 

152 

146 

145 

186 

149 

142 

125 

141 

141 

142 

140 

131 

35 

193 

140 

113 

24 

199 

101 

139 

130 

22 

130

1:~ge No. 

GUO, D 200 

GUO, W 196 

GUO, W 172 

HALL, L D 164 

HALL, L D 162 

HAMMEN, P K 169 

HAMMOND, T E 124 

HAN, J-W 150 

HANDSCHMACHER, R E 192 

HANER, R L 201 

HARBISON, G S 157 

HARDING, M W 192 

HARTMAN, J S 200 

HASENFELD, A 102 

HAWKINS, B L 201 

HAWKINS, B L 20 

HAYCOCK, J C 103 

HEALD, S L 192 

HEFFRON, G J 146 

HEINEKEY, M 185 

HELMS, G 162 

HELMS, G L 158 

HENRICHS, P M 116 

HENTSCHEL, D 126 

HILL, H 46 

HING, A 130 

HO, C 181 

HOFFMAN, R 152 

HOFFMAN, R E 144 

HOLLANDER, J D 179 

HORNAK, J P 148 

HORNAK, J P 149 

HOULT, D I 194 

HU, J 186 

HUANG, Y 196 

HUGHES, D W 127 

HUGHES, D W 108 

HUNTER, H N 127 

HWANG, Y C 104 

HYBERTS, S G 151 

HYMAN, T 143 

HYMAN, T J 145 

INGLEFIELD, P T 138 

IVERSON, D 117 

JACKSON, G 143 

JAKOBSEN, H J 123 

JANZEN, E G 183 

JARAMILLO, B 165 

JELINSKI, L W 61 

JELINSKI, L W 161 

JEONG, Y S 179 

JIANG, S 196 

JIANG, Y J 141 

JIN, H 198 

JOHNSON, C S 116 

JOHNSON, W C 192 

JOHNSTON, E R 177 

JONAS, J 111 

JONAS, J 186 

JONAS, J 175 

205 

JONAS, J 

JONES, A A 

JONES, C R 

JUE, T 

KAINOSHO, M 

KALNIK, M W 

KAMBOUR, R P 

KAPLAN, D 

KAPLAN, S 

KAY, L E 

KENDRICK, R D 

KENNEDY, M A 

KESHAVAN, M S 

KIM, S-G 

KIRBY, R A 

KNEIP, G 

KOHLER, S J 

KOHNO, H 

KOLBERT, A C 

KOLODNY, N H 

KOOK, A M 

KOUCHAKDJIAN, M 

KRAMER, D M 

KREZEL, A 

KUAN, W 

KUBAS, G 

KUHNS, P L 

KURLAND, R J 

KVALHEIM, 0 M 

LACELLE, S 

LADEBECK, R 

LAI, X 

LAPLANCHE, L A 

LAPLANTE, S 

LAPLANTE, S 

LAPLANTE, S R 

LEAHY, D J 

LED, J J 

LEE, C E 

LEE, C J 

LEE, J P 

LEE, S C 

LEO, G C 

LEO, G C 

LEOPOLD, M F 

LERNER, L 

LEUPIN, W 

LEVITT, M H 

LEVITT, M H 

LEVITT, M H 

LEVY, G 

LEVY, G C 

LEVY, G C 

LEVY, G C 

LEVY, G C 

LEVY, G C 

LEVY, G C 

LEVY, G C 

LEVY, G C 

LEVY, L A 

Page No. 

26 

138 

156 

191 

167 

136 

138 

181 

109 

128 

69 

187 

181 

104 

98 

46 

139 

112 

113 

139 

177 

136 

152 

167 

153 

185 

14 

145 

199 

172 

126 

155 

176 

144 

143 

146 

65 

120 

173 

159 

118 

106 

136 

137 

140 

36 

117 

38 

113 

24 

144 

146 

147 

100 

146 

152 

144 

103 

145 

178

LEWIS, B A 

LI, L 

LI, L 

LIAN, S 

LIM, T K 

LIMAT, D 

LIN, F M 

LIN, F T 

LIND, A C 

LINK, J 

LIPPMAA, E 

LIPTON, A S 

LISICKI, M 

LISTERUD, J 

LISTINSKY, J J 

LIU, G 

LIVE, D 

LIVE, D H 

LOCK, H 

LOGRASSO, P V 

LOGRASSO, P V 

LONDON, R E 

LOVY, J 

LUCK, L A 

LUYTEN, P 

LYONS, B 

MACDIARMID, A G 

MACDONALD, P M 

MACIEL, G E 

MACIEL, G E 

MACIEL, G E 

MACIEL, G E 

MACOVSKI, A 

MACUR, A 

MACURA, S 

MAEREFAT, N L 

MAJORS, P D 

MALSCH, K D 

MANASSEN, Y 

MARECI, T H 

MARECI, T H 

MARESCH, G G 

MARION, D 

MARION, D 

MARKLEY, J L 

MARKLEY, J L 

MARKLEY, J L 

MARKLEY, J L 

MARKLEY, J L 

MARKLEY, J L 

MARKLEY, J L 

MARKLEY, J L 

MARSHALL, E 

MARTIN, E S 

MARTIN, G 

MATEESCU, G 

MATSUI, S 

MATTINGLY, M 

MAYNE, C L 

MAYNE, C L 

Page No. 

165 

70 

115 

196 

193 

32 

150 

150 

188 

55 

114 

146 

183 

200 

149 

111 

61 

108 

70 

182 

182 

178 

153 

125 

179 

173 

109 

184 

70 

20 

115 

201 

59 

152 

167 

157 

184 

125 

138 

190 

190 

69 

178 

36 

166 

167 

158 

167 

166 

168 

168 

160 

149 

160 

143 

189 

112 

131 

141 

142 

206 

MAZZEO, A R 

MAZZOLA, L T 

MCCONNELL, H M 

MCCOY, M 

MCDANIEL, P L 

MCEVOY, J 

MCFADDIN, D 

MCNAMARA, R 

METZ, K R 

MICHL, J 

MILLAR, j 

MILLER, J B 

MILLER, J B 

MILLER, J B 

MILLER, j B 

MIRAU, P A 

MISHRA, P 

MONTELIONE, G T 

MOOBERRY, E S 

MOOBERRY, E S 

MOOBERRY, E S 

MOONEY, J R 

MOORE, R E 

MOORE, R E 

MORAT, C 

MORAT, C 

MORRIS, H D 

MOTTEN, A G 

MUELLER, L 

MUELLER, 0 M 

MULLER, S 

MUNTEAN, J V 

MURAKI, A 

MURPHY, M 

MYERS-ACOSTA, B L 

McCARRON, E M 

NAGAO, H 

NAGAYAMA, K 

NAKAI, T 

NAVON, G 

NELSON, S J 

NELSON, S J 

NEWMARK, R D 

NEWMARK, R D 

NICELY, V A 

NICHOLSON, L K 

NIELSEN, N C 

NIEMCZURA, W P 

NIEMCZURA, W P 

NIISAN, R A 

NIRMALA, N R 

NISHIMURA, D G 

NORMAN, D 

NORRIS, J R 

NORTH, C L 

O'BRIEN, P 

OH, BH 

OH, BH 

OLEJNICZAK, E T 

OPELLA, S J 

Page No. 

147 

62 

65 

102 

111 

181 

169 

132 

184 

125 

185 

170 

49 

171 

170 

161 

165 

148 

160 

158 

166 

124 

158 

162 

98 

120 

188 

178 

135 

194 

55 

98 

139 

107 

196 

129 

167 

115 

113 

138 

124 

123 

154 

154 

116 

182 

123 

158 

162 

99 

147 

59 

136 

107 

182 

127 

158 

168 

140 

132

OPELLA, S J 

ORENDT, A M 

OTTING, G 

PADMANABHAN, S 

PAFF, J 

PANCHALINGAM, K 

PAZARA, D 

PERPICK-DUMONT, M 

PERRIN, C L 

PERRIN, C L 

PETTEGREW, J 

PFANDLER, P 

PINES, A 

PINES, A 

PLANT, H D 

POULTER, C D 

PRATUM, T K 

PRESTEGARD, J H 



PRINS, K 0 

PUAR, M S 

PUGMIRE, R J 

PUGMIRE, R J 

PUGMIRE, R J 

~ IAN, B 

ABENSTEIN, D L 

RADZISZEWSKI, J G 

RALEIGH, D P 

RALEIGH, D P 

RALEIGH, D P 

RALEIGH, D P 

RAM, P 

RAM, .P 

RAMANATHAN, K V 

RATCLIFFE, C I 

RATCLIFFE, C I 

RECORD, M T 

REICHWEIN, A 

REILY, M D 

REMEIKA, J P 

REYNOLDS, W F 

RHEINGOLD, A L 

RICHARDSON, M F 

RICHTER, A F 

RINALDI, P 

RIPMEESTER, J A 

RIPMEESTER, J A 

RITCHEY, W M 

ROBERT, J M 

ROBERTSON, A D 

ROEMER, P B 

ROEMER, P B 

ROGGENBUCK, M W 

ROGGENBUCK, M W 

ROOS, M S 

ROOS, M S 

ROY, A K 

ROY, J 

RULE, G S 

Page No. 

161 

125 

117 

165 

101 

181 

189 

180 

176 

106 

181 

32 

18 

159 

109 

174 

169 

128 

127 

62 

198 

126 

149 

141 

141 

186 

172 

125 

155 

140 

24 

113 

127 

62 

132 

134 

98 

165 

50 

166 

45 

180 

125 

200 

109 

117 

98 

134 

174 

192 

167 

57 

194 

146 

145 

154 

154 

138 

197 

65 

207 

RUSSELL, A F 

RUTAR, V 

SAARINEN, T R 

SAMMONS, R D 

SAMMONS, R D 

SAMOSON, A 

SANCTUARY, B C 

SANDERS, J K M 

SANDERS, J P 

SANTINI, R 

SARKAR, S K 

SCHAEFER, J 

SCHAEFER, J 

SCHAEFER, J 

SCHLEICH, T 

SCHONENBERGER, C 

SCHROEDER, S A 

SEELIG, J 

SEKIHARA, K 

SELINSKY, B S 

SELOVER, S J 

SETHI, N K 

SHAKA, A J 

SHALWITZ, R A 

SHANMIN, Z 

SHERRIFF, B L 

SHERWOOD, M H 

SHERWOOD, M H 

SHIONO, H 

SHIRLEY, W M 

SHOOP, J D 

SHRIVASTAVA, P N 

SHUKLA, R 

SHUNGU, D C 

SIKORSKI, J A 

SILVER, L A 

SIMONDS, M A 

SIMPLACEANU, V 

SKLENAR, V 

SLETTEN, E 

SLICHTER, C P 

SLOMP, G 

SMITH, C D 

-SMITH, C D 

SMITH, E 

SMITH, K A 

SMITH, M E 

SMITH, S L 

SMITH, S L 

SOFFE, N 

SOLE, P 

SOLE, P 

SOLUM, M S 

SORENSEN, 0 W 

SOTAK, C H 

SPANTON, S G 

SPARKS, S W 

SPIKER, D 

STARK, R E 

STENGLE, T R 

Page No. 

106 

99 

116 

137 

136 

114 

102 

30 

114 

156 

131 

22 

130 

130 

201 

35 

156 

55 

112 

178 

196 

149 

159 

104 

119 

101 

142 

141 

112 

110 

145 

165 

183 

189 

137 

159 

195 

181 

39 

199 

44 

100 

163 

163 

172 

105 

179 

163 

163 

137 

152 

100 

149 

123 

156 

135 

164 

181 

112 

195

STEPHENS, R L 

STIPANOVIC, A J 

STOCK, L M 

STOCKMAN, B J 

STOCKMAN, B J 

STOLPER, E M 

STOY, V 

STRUB, H 

STUART, J A 

SUDMEIER, J L 

SZEVERENYI, N M 

TABER, K H 

TALAGALA, S L 

TANG, J 

TARAVEL, R F 

TAYLOR, J S 

TENG, Q 

TERAO, T 

THANABAL, V 

THOBURN, J D 

THOMA, W J 

THOMANN, H. 

THOMANN, H 

THOMAS, G S 

THOMAS, G S 

THOMPSON, A R 

THOMPSON, G 

TINDALL, P J 

TOMONAGA, N 

TORCHIA, D A 

TORCHIA, D A 

TORGESON, D R 

TOWNER, R A 

TSAIO, C 

TSCHUDIN, R 

TSIAO, C 

TUTUNJIAN, P N 

TYCKO, R 

ULRICH, E L 

VAN DER PUTTEN, D 

VAN OS, J W M 

VAN ZIJL, P C M 

VANDERAH, T A 

VANDERVELDE, D 

VEEMAN, W S 

VEGA, A J 

VETTER, J 

VINEGAR, H J 

WAGNER, G 

WAGNER, G 

WAGNER, G 

WAGNER, G 

WALKER, N A 

WALSH, C T 

WALSTEDT, R E 

WAMBABE, C 

WANG, C 

WANG, D 

WANG, G 

WANG, J 

Page No. 

135 

175 

98 

160 

158 

159 

153 

125 

173 

38 

131 

111 

162 

107 

120 

123 

182 

113 

134 

176 

123 

198 

197 

163 

163 

191 

179 

197 

167 

164 

180 

150 

183 

28 

36 

197 

194 

128 

166 

198 

50 

183 

99 

186 

50 

129 

126 

194 

134 

148 

147 

151 

186 

193 

45 

139 

118 

186 

186 

168 

208 

WANG, P C 

WANG, S 

WARREN, W S 

WARREN, W W 

WATERHOUSE, A 

WATERHOUSE, A L 

WAUGH, J S 

WEBB, A G 

WEBB, G G 

WEBER, P L 

WEISERMAN, L F 

WEISS, R G 

WENCKEBACH, W Th 

WESTLER, W M 

WESTLER, W M 

WESTLER, W M 

WESTLER, W M 

WEYAND, J D 

WHITE, D 

WHITE, D 

WHITTENBURG, S L 

WILD, C 

WILD, C 

WILKINSON, D A 

WILLIAMS, P G 

WILLIAMSON, K L 

WILLIAMSON, K L 

WIMPERIS, S 

WIND, R A 

WIND, R A 

WIND, R A 

WOLF, G E 

WONG, S T S 

WONG, S T S 

WOO, K W 

WOOLFENDEN, W R 

WOOLFENDEN, W R 

WU, G 

WU, X L 

WU, X W 

WUTHRICH, K 

XIAOLING, W 

XIE, C-L 

XUEWEN, W 

YAMANE, T 

YAN, X 

YANG, T S 

YANNONI, C S 

YANNONI, C S 

YESINOWSKI, J P 

YOUNG, R H 

YU, C 

YUAN, B 

YVARS, G 

ZAGORSKI, M G 

ZENG, Y 

ZENS, T 

ZHANG, S M 

ZILM, K 

ZILM, K W 

Page No. 

139 

144 

102 

45 

133 

133 

14 

164 

185 

135 

160 

129 

67 

160 

168 

167 

166 

53 

173 

107 

192 

28 

197 

165 

202 

195 

195 

32 

70 

115 

20 

181 

154 

154 

175 

149 

141 

196 

122 

122 

117 

119 

186 

119 

61 

186 

174 

69 

28 

159 

115 

118 

158 

189 

136 

107 

152 

122 

185 

185

ZLOTNIK-MAZORIo T 

ZUMBULYADIS, N 

Page No. 

112 

115 

209

William Abraham 

University of Iowa 

270 Med Labs 

Iowa City, IA 52242 

Telephone: 314 335-8078 

Connie Ace 

Ethicon Inc. 

Route 22 

Somerville, NJ 08876 

Telephone: 201 218-3036 

Jerome L. Ackerman 

Mass General Hospital 

Dept. of Radiology 

Boston, MA 02114 

Telephone: 617 726-3083 

Joseph J.H. Ackerman 

Dept of Chemistry, Box 1134 

University of Washington 

St. Louis, MO 63130 

Telephone: 314 889-6357 

Bruce Adams 

Univ of Wisconsin 

1101 University Avenue 

Madison, WI 53706 

Telephone: 608 262-3182 

Michael J. Albright 


186 Wood Ave. South 

Iselin, NJ 08830 

Telephone: 201 632-2884 

Dr. James L. A1derfer 

Roswell Park Memorial Inst. 

Biophysics Dept. 

Buffalo, NY 14263 

Telephone: 716 845-4471 

Donald W. Alderman 

Chemistry Dept 

Univ of Utah 

Salt Lake City, UT 84112 

Telephone: 80i 581-7184 

Lawrence Alemany 

Mobil Research & Development 

Billingsport Road 

Paulsboro, NJ 08066 

Telephone: 609 423-1040 

Willi Ammann 


611Hansen Way 

Palo Alto, CA 94303 

Telephone: 415 493-4000 

George Anastasi 

Mannlng Park 

Bruker Instruments, Inc 

Billerica, MA 01821 

Telephone: 617 667-9580 

Niels H. Andersen 

Univ. of Washington 

Dept. of Chemistry 

Seattle, WA 98195 

Telephone: 206 543-7099 

A. M. (ANDY) Anderson 

Wilmad Glass Co. Inc. 

Rte. 40 & Oak Road 

Buena, NJ 08310 

Telephone: 805 492-5808 

John A. Anderson 

University of Illinois 

PO Box 69~8-M/C 937 

Chicago, I[ 60680 

Telephone: 312 996-6640 

Mark Anderson 

Univ of Wisconsin-Madison 

420 Henry Mall 


Telephone: 608 262-4687 

William R. Anderson 

Lehigh University 

S. G. Mudd Building #6 

Bethlehem, PA 18015 

Telephone: 215 758-3465 

Clemens Anklin 

Manning Park 

Bruker Instruments, Inc 


Telephone: 617 667-9580 

Byron Arison 

Merck & Co. 

P.O. Box 2000 

Rahway, NJ 07065 

Telephone: 201 574-5394 

Dr. lan M. Armitage 

Yale University 

PO Box 3333-333 Cedar Street 

New Haven, CT 06510 

Telephone: 203 785-4443 

David A. Armour 

Siemens Medical Systems, Inc. 

186 Wood Avenue South 


Telephone: 201 321-4832 

Robert D. Armstrong 


255 Fourier Avenue 

Fremont, CA 94539 

Telephone: 415 683-4408 

Henry C Arndt 

Miles Inc 

1127 Myrtle St 

Elkhart, IN 46514 

Telephone: 219 262-7692 

Joseph Ashcroft 

Rockefeller University 

1230 York Ave 

New York, HY 10021-6399 

Telephone: 212 570-7589 

Albert Attalla 

Monsanto Research Corp 

Mound Road 

Miamisburg, OH 45342 

Telephone: 513 865-3454 

Hector E. Avram 

Diasonics MRI 

400 Grandview Drive 

South San Francisco, CA 94080 

Telephone: 415 952-1366 

Alvin C. Bach 

E I Dupont Med Products 

Experimental Station E336/029 

Wilmington, DE 19898 

Telephone: 302 695-3306 

Dave H Badtke 


255 Fourier Ave 


Telephone: 415 683-4342

David B. Bailey 

USI Chemicals Co. 

1275 Section Rd. 

Cincinnati, OH 45237 

Telephone: 513 761-4130 

Alex D. Bain 

McMaster University 

1280 Main St. W. 

Hamilton, Ont., L8S 4MI 

CANADA 

Telephone: 416 525-9140 

Laima Baltusis 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Ben W Bangerter 

Dept of Chem; Yale Univ 

225 Prospect St; PO Box 6666 


Telephone: 203 432-3942 

Edmund L. Baniak 

Texaco Inc 

PO Box 509 

Beacon, NY 12508 

Telephone: 914 831-3400 

Shelton Bank 

State Univ of New York 

1400 Washington Avenue 

Albany, NY 12222 

Telephone: 518 442-4447 

Daniel J. Barabino 

Pennsylvania State Universit) 

Dept of Chemical Engineering 

University Park, PA 16802 

Telephone: 814 865-1261 

Thomas Barbara 

Suny; Dept of Chem 

Stony Brook, NY 11794 

Telephone: 516 632-7991 

Dr. Gareth J Barker 

University of Florida 

Box J-374, JHMHC 

Gainesville, FL 32610 

Telephone: 904 392-3087 

Mufeed M. Basti 

Northern Illinois University 

820 Kimberly Drive, #201 

DeKalb, IL 60115 

Telephone: 815 753-1131 

Vladimir J Basus 

Univ of California 

School of Pharm; Box 0446 

San Francisco, CA 94143 " 

Telephone: 415 476-3027 

Lynne S. Batchelder 


1120 Auburn Street 


Telephone: 415 659-2600 

Lorenz Bauer 

Allied Signal EMRC 

50 E. Algonquin Rd. 

Des Plaines, IL 60017 

Telephone: 312 391-3381 

Mary W. Baum 




Telephone: 609 987-2902 

Ad Bax 

Natl Institute of Health 

Bldg. 2, Rm 109 

Bethesda, MD 20892 

Telephone: 301 496-2848 

Renzo Bazzo 

Dept. of Biochemistry 

Oxford Univ. 

Oxford, England, 

OX1 3QR U.K. 

Telephone: 0865 275720 

William H Bearden 

JEOL USA INC 

11 Dearborn Rd 

Peabody, MA 01960 

Telephone: 617 535-5900 

William T. Beaudry 

US Army Chem Res Dev & Eng Ctr 

Attn: SMCCR-RSC-P/Beaudry 

Aberdeen Proving Grd, MD 21010-5423 

Telephone: 301 671-3863 

Edwin D. Becker 

National Institutes of Health 

Bldg. I/Room 118 


Telephone: 301 496-2215 

Nancy N. Becker 

Washington Univ-Dept of Chem 

Box 1134-I Brookings Drive 


Telephone: 314 889-6583 

Alvin Beeler 

E.I. DuPont de Nemours 


Wilmington, DE 19898 " 

Telephone: 302 695-4595 

John H. Begemann 


719 East Genesee St. 

Syracuse, NY 13210 

Telephone: 315 424-0329 

Ron Behlin 

AT&T Bell ~aboratories 

IC-432, 600 Mountain Avenue 

Murray Hill, NJ 07974-2070 

Telephone: 201 582-4719 

Russell A. Bell 


Hamilton, Ontario, 

CANADA 

L8S 4MI 

George M Benedikt 

BF Goodrich 

9921Brecksville Road 

Brecksville, OH 44141 

Telephone: 216 447-5448 

Alan Benesi 

Pennsylvania State University 

152 Davey Lab-Chemistry Dept. 


Telephone: 814 865-0941 

Donald G. Bennett 

Carnegie Mellon University 

4400 5th Avenue, Mellon Inst. 

Pittsburgh, PA 15213 

Telephone: 412 268-3161

\ , 

Lawrence Bennett 


600 Clemson Road 

Columbia, SC 29223 

Telephone: 803 788-6497 

Mabry Benson 

Western Regional Lab - USDA 

800 Buchanan Street 

Albany, CA 94610 

Telephone: 415 559-5757 

Debra Berg 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Wolfgang Bermel 


Manning Park 

Billerlca, MA 01821 

Telephone: 617 667-9580 

Michael Bernstein 

Merck Frosst Canada, Inc. 

P.O. Box 1005 

Pointe Claire-Dorval, HgR 4P8 

CANADA 

Telephone: 514 695-7920 

Richard Bertrand 

Dept of Chemistry, PO Box 7150 

Univ of Colorado 

Colorado Springs, CO 80933-7150 

Telephone: 303 593-3139 

Serge Berube 

Univ De Sherbrooke Chimie 

2500 Boul. Universite 

Sherbrooke, Quebec, JIK 2RI 

CANADA 

Telephone: 8198217000x3099 

Kebede Beshah 

MIT/Magnet Lab 

77 Mass Ave 

Cambridge, MA 02139 

Telephone: 617 253-0258 

Norman Bhacca 

Chemistry Department 

Louisiana State University 

Baton Rouge, LA 70803 

Telephone: 504 388-3356 

Roy Bible 

G.D. Searle & Co. 

4901Searle Parkway 

Skokie, IL 60077 

Telephone: 312 982-7787 

Anthony Bielecki 

MIT, National Magnet Lab 

77 Massachusetts Avenue 


Telephone: 617 253-7561 

Glen Bigam 


University of Alberta 

Edmonton, Alberta, T6G 2G2 

CANADA 

Telephone: 403 432-2573 

Karl Bishop 

Syracuse University 

306 Bowne Hall 


Telephone: 315 423-1021 

Barbara A. Blackwell 

Agriculture Canada, C.E.F. 

Plant Res Ctr~ Research Branch 

Ottawa, Ontarlo, KIA OC6 

CANADA 

Telephone: 61399537007554 

C. Scott Blackwell 

Union Carbide Corp. 

Old Sawmill River Rd. 

Tarrytown, NY 10591 

Telephone: 914 789-3678 

Susan L. Blake 

Chemistry Dept. 

Queen's University 

Kingston, Ont., K7L 3N6 

CANADA 

Telephone: 613 547-6180 


Max Planck Inst Poiymerfosch 

Postfach 3148 

D-6500 Mainz, 

F.R. GERMANY 

Michael Blumenstein 

Hunter College 

695 Park Avenue 

New York, NY 10021 

Telephone: 212 772-5337 

Jo-Anne Bonesteel 

DuPont Experimental Station 

PPD E269/200 


Telephone: 302 772~1076 

Phillip Borer 



Syracuse, NY 13244-1200 

Telephone: 315 423-1021 

Vincent P. Bork 


Washington Univ. 


Telephone: 314 889-4665 

Marie Borzo 

Hoechst Celanese Res Division 

86 Morris Avenue 

Summit, NJ 07901 

Telephone: 201 522-7969 

Coleen Bosch 

Washington University 

1Brookings Drive, Box 1134 


Telephone: 314 889-6583 

A.A. Bothner-By 

Carne~gieTMellon Univ 

qquu rlftn ~ve. 


Telephone: 412 268-3125 

Robert E. Botto 

Chem. F189 

Argonne Natlional Lab 

Argonne, IL 60439 

Telephone: 312 972-3524 

Donald Bouchard 


Univ of Pennsylvania 

Philadelphia. PA 19104 

Telephone: 215 898~4886 

Ellis Boudreau 




Telephone: 315 423-I021

Yvan Boulanger 

Univ de Montreal 

Inst. Genie Biomedical CP 6128 

Montreal, Quebec, H3C 3J7 

CANADA 

Telephone: 514 343-6369 

Jonathan Boyd 

University of Oxford 

South Parks Road 

Oxford, 

U.K. OXl 3QU 

Telephone: 44 865-275335 

Robert D. Boyer 

B P America 

4440 Warrensville Center Road 

Cleveland, OH 44128 

Telephone: 216 581-5537 

Joel Bradley 

Cambridge Isotope Labs 

20 Commerce Way 

Woburn, MA 01801 

Telephone: 617 938-0067 

Raymond Brambilla 

Allied-Signal Corp 

Post Office Box I021R 

Morristown, NJ 07960 

Telephone: 201 455-2984 

Anita Brandolini 

Mobil Chemical Co. 

PO Box 240 

Edison, NJ 08818 

Telephone: 201 321-6288 

Amy Braveman 

University of Rochester 

Strong Mem Hosp, Biophy Dept 


Telephone: 716 275-8268 

Trond Brekke 

University of Bergen 


5007 Bergen, 

NORWAY 

Telephone: 05 213356 

Richard W. Briggs 

Univ of FL-Dept of Radiology 

Box J-374 


Telephone: 904 392-3087 

Douglas E. Brown 

Eastmen Kodak 

Kodak Park Bldg.82C 


Telephone: 716 477-6469 

Dr. Rodney D Brown 

IBM Research 

PO Box 218, Loc 26-250 

Yorktown Heights, NY 10598 

Telephone: 914 945-2320 

L.R. Brown 

Australian National University 

Res Sch of Chem, GPO Box 4 

Canberra, ACT 2601, 

AUSTRALIA 

Telephone: 062 49-3771 

Leo Brown 




Telephone: 415 683-4408 

Truman R. Brown 

Fox Chase Cancer Center 

7701Burholme Ave. 


Telephone: 215 728-3049 

Robert G. Bryant 

Biophysics Dept. Box BPHYS 



Telephone: 716 275-4877 

G. W. Buchanan 


Carelton University 

Ottawa, Ont., KIS 5B6 

CANADA 

Telephone: 613 564-2723 

Dr. David E. Bugay 

E. R. Squibb & Sons 

Rte. I @ College Farm Road 

New Brunswick, NJ 08903 

Telephone: 201 519-3211 

Dr. S. Bulusu 

US Army ARDEC 

Building 3028 

Dover, NJ 07801 

Telephone: 201 724-6450 

Lowell J. Burnett 

Physics Department 

San Diego State University 


Telephone: 619 265-3006 

Deborah Burstein 

Beth Israel Hospital 

330 Brookline Ave 


Telephone: 617 735-3349 

Douglas P. Burum 


Manning Park 


Telephone: 617 667-9580 


Biophysics/FDA/NIH 

8800 Rockville Pike 

Bethesdao MD 20892 

Telephone: 301-496-2542 

Sean M. Cahill 

Hunter College 

Chem Dept/695 Park Avenue 


Telephone: 212 772-5337 

Dale Campau 

Dow Chemical USA 

P.O. Box 400/Bldg. 2503 

Baton Rouge, LA 70765-0400 

Telephone: 504 389-6559 

Steve Caravajal 

Procter and Gamble 

5299 Spring Grove Ave 


Telephone: 513 627-5005 

Keith R. Carduner 

Ford Motor Co. 

925 N Elizabeth ST. 

Dearborn, MI 48128 

Telephone: 313 337-5454 

James L. Carolan 

Nalorac Cryogenics Corp. 

837 Arnold Dr., Ste. 600 

Martinez, CA 94553 

Telephone: 415 229-3501

J~ 

W. Robert Carper 

Wichita State University 


Wichita, KS 67208 

Telephone: 316 689-3120 

Stephen Castellino 

Monsanto 

Mail Zone U3D, 800 N Lindbergh 


Telephone: 314 694-4457 

Franco Cau 

Univ De Sherbrooke Chimie 

2500 Boulevard de l'Univ Sherb 

Sherbrooke, Quebec, JIK 2Rl 

CANADA 

Telephone: 8198217000x3099 

Toni L. Ceckler 

Univ. of Rochester Med Center 

Biophysics Dept - Box BPHYS 


Telephone: 716 275-4378 

V.P. Chacko 

Johns Hopkins Med Institutions 

MRI-110, 600 North Wolfe St 

Baltimore, MD 21205 

Telephone: 301 955-4220 

Jar-Bee Chan 

Univ of Illinois/Champaign 

505 S. Mathews, 24-I NL 

Urbana, IL 61801 

Telephone: 217-333-3897 

S. Chandrasekar 

Dept of Chemistry, Univ Plaza 

Georgia State Un)v 


Telephone: 404 651-3120 

Lydia L. Chang 

ICI Americas, Inc. 

1200 S. 47th Street 

Richmond, CA 94804 

Telephone: 415 231-1043 

Shoumo Chang 


UC Irvine 

Irvine, CA 92717 

Telephone: 714 856-6010 

Mohan V. Chari 

Baylor College of Med, MRI Ctr 

9450 Grogan's Mill Road 

Woodlands, TX 77380 

Telephone: 713 363-4844 

Mark Chaykovsky 


Mannin~ Park 


Telephone: 617 667-9580 

Deng-Ywan Chen 


Univ. of Pennsylvania 


Telephone: 215 898-4886 

Shiow-Meei Chen 

Univ of Wisconsin - Milwaukee 

3210 North Cramer Street 

Milwaukee, WI 53201 

Telephone: 414 229-5220 

Wenqiao Chen 

Hunter College, Cuny 

695 Park Ave 


Telephone: 212 772-5337 

Doris Chen~ 

Exxon Chemical Co 

1900 W. Linden Ave 

Linden, NJ 07036 

Telephone: 201 474-2591 

Guang-Qiang Chen 9 

Syracuse Universlty 

Bowne Hall 


Telephone: 315-423-1021 

Jung Tsang Cheng 

Chemistry Department. #26 



Telephone: 803 765-0247 

Gwendol~n N. Chmurny 

NCI-FCRF 

PO Box B. Bldg. 469, Rm. 162 

Frederick, MD 21701 

Telephone: 301 698-1226 

Shin-Il Cho 




Telephone: 803 788-6497 

Ashok Cholli 

BOC Group 

100 Mountain Ave 

Murray Hill, NJ 07974 

Telephone: 201 464-8100 

Kenner Christensen 

Univ of Arizona 

Chem Dept 

Tucson, AZ 85721 

Telephone: 602 621-2308 

Po-Jen Chu 

Texas A&M University 

Dept of Chem, Room 2407 

College Station, TX 77840 

Telephone: 409 845-8299 

Simon Chu 




Telephone: 415 659-2600 

Ted Claiborne 

MedRad Inc 

Post Office Box 730 

Indianola, PA 15051 

Telephone: 412 767-9877 

Mike C1ingan 

Doty Scientific, Inc. 



Telephone: 803 788-6497 

David W. Cochran 

Wyeth-Ayerst Research 

CN 8000 


Telephone: 201 274-4481 

Michael D. Cockman 


Box 71, Leigh Hall 


Telephone: 904 392-3087

Helga Cohen 

Univ of So Carolina 

Chem Dept NMR Facility 


Telephone: 803 777-2649 

Holly Cole 


Building 30 Room 106 


Telephone: 301 496-6307 

Lawrence D Colebrook 

Concordia Univ, Chem Dept 

1455 deMaissoneuve Blvd W 

Montreal, Quebec, H3G IM8 

CANADA 

Telephone: 514 848-3336 

Kim Colson 

Bristol-Myers Company 

Analy Chem-5 Research Parkway 

Wallingford, CT 

Telephone: 203 284-7535 

James W. Cooper 

IBM 

472 Wheelers Farm Rd. 

Milford, CT 06460 

Telephone: 203 783-4536 

Paul Cope 

Wilmad Glass Co., Inc. 

Route 40 & Oak Rd. 


Telephone: 609 697-3000 

Valerie Copie 

Mass Institute of Technology 

170 Albany Street. NW 14-5111 


Telephone: 617 253-5416 

Chris Coretsopoulos 

Univ of II; Box 24 Noyes Lab 

505 South Mathews 

Urbana-Champaign, IL 61821 

Telephone: 217 333-5544 

Mary Lou Cotter 

Ortho Pharmaceutical Corp 

Route 202 - Box 300 

Raritan, NJ 08869-0602 

Telephone: 201 218-6292 

Charles E. Cottrell 

Ohio State University 

120 West 18th Avenue 

Columbus, OH 43210 

Telephone: 614 292-0489 

S. H. Couturie 

Chevron Oil Field Research Co. 


La Habra, CA 90633-0446 

Telephone: 213/694-9332 

David Cowburn 


1230 York Avenue 

New York, NY 10021-6399 

Telephone: 212 570-8270 

Bruce Coxon 

National Bureau of Standards 

Chemistr~ Bldg. A361 

Gaithersburg. MD 20899 

Telephone: 301 975-3135 

Madeleine H. Cozine 

Yale Univ-Sterling Chem Labs 

225 Prospect Street 


Telephone: 203 432-3933 

Ray Crandall 

Xerox Corp 

800 Phillips Rd 

Webster, NY 14580 

Telephone: 716 422-1797 

Roger W Crecely 

Unlv of Delaware 

Chem Dept 

Newark, DE 19716 

Telephone: 302 451-8901 

R. William Creekmore 

FMC Corporation 

PO Box 8 


Telephone: 6094522300x4391 

F J Creuzet 

Nat'l Magnet Lab, MIT 

77 Mass Ave, B1dg NW14-5107 


Telephone: 617 253-5586 

William R. Croasmun 

Kraft Research & Development 

801Waukegan Rd. 

Glenview, IL 60025 

Telephone: 312 998-3647 

Beth A. Crockett 

Dept of Chemistry 

Univ of S Carolina 


Telephone: 803 777-7399 

Bob Crosby 

M-R Resources Inc 

38 Parker Street 

Gardner, MA 01440 

Telephone: 617 632-7000 

Timothy Cross 

Florida State University 


Tallahassee, FL 32306-3006 

Telephone: 904 644-2824 

Michael Crowley 

Harper Hospital/MR Center 

3990 John R 

Detroit, MI 48201 

Telephone: 313 745-1379 

Molly Crowther 


719 E. Genesee Street 


Telephone: 315 423-0329 

Phillip Cruz 

Wright State University 

Dayton, OH 45435 

Telephone: 513 873-2024 

Janet Curtis 

University of Utah 

210 Park Building 

Salt Lake City, DT 84112 

Telephone: 801 581-7351 

John D. Cutnell 

Dept. of Physics 

Southern Illinois University 

Carbondale, IL 62966 

Telephone: 618 453-3735

Andre D'Avignon 

• Dept. of Chemistry Box 1134 


St LOUlS, MO 63130 

~elephone: 318 889-4715 

Dr. Josef Dadok 


4400 Fifth Avenue 


Telephone: 412 ~68-3146 

Jerry L. Dallas 


255 Fourier Ave. 


Telephone: 415 683-4363 

Neal Dando 

ALCOA 

Rt 780 Alcoa Technical Ctr 

Alcoa Center, PA 15069 

Telephone: 412 337-5367 

Charles Danehey 

Union Carbide 

Old Saw Mill River Road 

Tarrytown, NY 10591 

Telephone: 914 789-3235 

Prashanth Darba 


Dept of Biochem-Natl Nag Reso 


Telephone: 608 263-9494 

Donald G. Davis 

Natl Inst of Env Hlth Sciences 

Box 12233; MD 5-01 

Research Triangle, NC 27709 

Telephone: 919 541-1986 

Nicolette Davis 

1280 Walnut Avenue, #68 

Tustin, CA 92680 

Telephone: 714 544-4035 

Brian Dawson 

Health & Welfare Canada 

Banting Bldg( Tunney's Pasture 

Ottawa/Ontario, KIA O12 

CANADA 

Telephone: 613 957-1068 

William H. Dawson 

CANMET - Department of Energy 

555 Booth Street 

Ottawa/Ontario, KIA OGI 

CANADA 

Telephone: 613 996-5298 

A. De Groot 

Koninklyke Shell Lab Amsterdam 

Badhuisweg 3 Post Bus 3003 

1003 AA Amsterdam, 

THE NETHERLANDS 


Huub J. M. De Groot 

Francis Bitter Lab/NIT 

170 Albany Street 


Telephone: 617 253-0962 

Jeff De Ropp 

NMR Facility 

UC Davis 

Davis, CA 95616 

Telephone: 916 752-7677 

Paul A. DeMuth 

Univ of Rochester-Biophysics 

Strong Memorial Hospital 


Telephone: 716 275-4378 

James J. Oechter 

Arco Oil & Gas, Co. 

2300 W. Piano Pkwy 

Piano, TX 75075 

Telephone: 214 754-6607 

Alan J. Deese 



Freemont, CA 94539 

Telephone: 415 683-4408 

Frank Delaglio 

New Methods Research Inc. 

719 East Genesee Street 


Telephone: 315 424-0329 

John Delayre 

TECMAG 

6006 Bellaire Blvd. 

Houston, TX 77081 

Telephone: 713 667-1507 

Peter C. Demou 


Chemistry Dept. PO Box 6666 


Telephone: 203 432-3940 

Heather D Dettman 

Univ of Ottawa; Chem Dept 

32 George Glinski 

Ottawa/Ontario, KIN 6N5 

CANADA 

Telephone: 613 564-7894 

Lisa A. Deuring 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415-493-4000 

Alice Oi Gioia 

Ashland Chemical Company 

PO Box 2219 


Telephone: 614 889-4597 

Lisa DiMichele 

Merck & Co, Inc. 

PO Box 2000; R801-210 


Telephone: 201 574-7139 

Dr. Joseph A D/Verdi 

Chemagnetics Inc 

208 Commerce Drive 

Ft. Collins, CO 80524 

Telephone: 303 484-0428 

Frank J. D/nan 

Occidental Chemical Corp 

2801 Long Road 

Grand Island, NY 14072 

Telephone: 716 773-8607 

Peter J. Oomaille 




Telephone: 302 695-2723 

Harr~ C. Dorn 

Virglnla Tech 

Chem Oept 

Blacksburg, VA 24061 

Telephone: 703 961-5953

F. David Doty 

Doty Scientific Inc. 



Telephone: 803 788-6497 

Judy Doty 

Doty Scientific Inc. 



Telephone: 803 788-6497 

Daryl A. Doughty 

Natl.lnst for Petro & Engy Kes 

220 N Virginia Ave, POBox 2128 

Bartlesville, OK 74005 

Telephone: 918336-2400X296 

Daniel R Draney 

American Cyanamid Co. 

1937 W. Main St. 

Stamford, CT 06904 

Telephone: 203 348-7331 

Gary Drobny 


Department of Chemistry, BG-IO 


Telephone: 206 545-2052 

Maureen A. Duffy 




Telephone: 617 938-0067 

R. William Dunlap 

Amoco Research Center 

PO Box 400 

Naperville, IL 60566 

Telephone: 312 420-5154 

Lois J. Durham 

Stanford Univ 

Chem Dept 

Stanford, CA 94305 

Telephone: 415 723-1610 

April Dutta 

Resonex Inc 

720 Palomar Avenue 

Sunnyvale, CA 94086 

Telephone: 408 720-8600 

Tammy J. Dwyer 

Univ of. California, San Diego 

Dept of Chem-Mail Code DO06 

La Jolla, CA 92093 

Telephone: 619 534-3173 

Cecil Dybowski 

Dept. of Chem. & Biochem. 

University of Delaware 

Newark, DE 19716 

Telephone: 302 451-2726 

Thomas A. Early 




Telephone: 415 683-4364 

Margaret A. Eastman 

Baker Lab of Chemistry 

Cornel Ithacal University 

NY 14853-1301 

Telephone: 607 255-4860 

Hugh L. Eaton 

Unlv of Wash, Biomembrane Inst 

201 Elliot Avenue, West 


Telephone: 206 545-2086 

Hellmut Eckert 

UC Santa Barbara 


Goleta, CA 93106 

Telephone: 805 961-8163 

Richard Eckman 

Exxon Chemical Company 

5200 Bayway Drive 

Baytown, TX 77520 

Telephone: 713 425-2474 

Heinz Egloff 




Telephone: 415 659-2600 

Keiji Eguchi 

JEOL USA INC 

II Dearborn Rd 


Telephone: 617 535-5900 

Irena Ekiel 

National Research Council 

100 Sussex Drive 

Ottawa, Ontario, KI~ OR6 

CANADA 

Telephone: 613 990-0905 

Paul D. Ellis 




Telephone: 803 777-6490 

Carl Engelman 

Ohio State University 

120 West 18th Avenue 


Telephone: 614 292-8625 

Helen R. Engeseth 

GE Medical Systems 

W-804, Post Office Box 414 


Telephone: 414 521-6338 

Alan D. English 

EI DuPont de Nemours & Co. 

Experimental Station 


Telephone: 302 695-4851 

Raul G. Enri~u?z. 

Facultad de Hulmlca Unam 

Oiv. Est. Posgrado 

Mexico City, 

20 DF MEXICO 

Telephone: 905 658-9534 

George Entzminger 


600 Clemson Rd. 


Telephone: 803 788-6497 

C. Anderson Evans 

Schering Corporation . 

86 Orange Street (B-9-B) 

Bloomfield, NJ 07003 

Telephone: 201 429-3957 

Frederick E. Evans 

Natl Center for Tox. Res. 

HFT 110 

Jefferson, AR 72079 

Telephone: 501 541-4317

Edward Ezell 

Dept HBC&G, F-20;3.362 GB B4dg 

Univ of Texas 

Galveston, TX 77550 

Telephone: 409-761-3997 

Fouad Ezra 

Proctor & Gamble Miami Valley 

PO Box 398707 


Telephone: 513 245-2485 

Kevin L. Facchine 

ORTHO Pharmaceutical Corp. 

Route 202 

Raritan, NJ 08869 

Telephone: 201 218-6230 

Paul E. Fagerness 

The Upjohn Co. 

Prod Contr II, MS 4822-259-12 


Telephone: 616 329-3931 

Liu Fan 9 

Universlty of Utah 



Telephone: 801 581-7351 

Rod Farlee 

DuPont Central Research 

Experimental Station 328 


Telephone: 302 669-1757 

Sandy Farmer 


611Hansen Way 


Telephone: 415 493-4000 

lan Farnan 

Stanford University 

Department of Geology 


Telephone: 415 723-3831 

Margaret R. Farrar 

Nat Rag Lab/Brandeis Univ 

HIT NW14-5107, 170 Albany St. 


Telephone: 617 253-5586 

Timothy R. Fennell 

Chem Ind Inst of Toxicology 

P 0 Box 12137 

Research Triangle Pk, NC 27709 

Telephone: 919 541-2070 

James Ferretti 


Bldg 10 Room 7N315 


Telephone:, 301 496-3341 

Morton A. Fineman 

Physics Dept. 

San Diego State Univ. 


Telephone: 619 265-4326 

Kenneth W. Fishbein 

Nat1 Magnet Lab, M.I.T. 



Telephone: 617 253-5586 

Jeffrey Fitzsimons 


J-374 JHMHC 


Telephone: 904 395-0293 

William W. Fleming 

IBM Almaden Research Center 

K91/801; 650 Harry Rd. 

San Jose, CA 95120-6099 

Telephone: 408 927-1611 

Charles E. Forbes 

Hoechst Celanese 

86 Morris Ave 


Telephone: 201 522-7913 

Jeffrey Forbes 

Box 42, 505 S. Mathews 

Univ of Illinois 


Telephone: 217 333-3004 

Joseph J. Ford 

Baylor College of Medicine 

9450 Grogan's Mill Road 

Woodlands, TX 77380 

Telephone: 713 363-4844 

Hans Forster 


Mannin~ Park 


Telephone: 617 667-9580 

Natalie Foster 

Lehigh Univ 

• Dept of Chem Mudd Bldg @6 


Telephone: 215 758-3646 

Jocelyn Fowler 

Univ of Pennsylvania-Dept Chem 

34th & Spruce Streets 


Telephone: 215 898-4886 

David Foxall 




Telephone: 415 659-2600 

Anne Frederick 


Dept of Chem-225 Prospect St. 


Telephone: 203 432-3992 

James E. Freeman 

The Upjohn Company 

M.S. 4820-259-12 


Telephone: 616 323-4103 

Michael A Freeman 

Exxon Res. and Dev Labs 

PO Box 2226 


Telephone: 504 359-4444 

Ray Freeman 

Dept Phys Chem., Lensfield Rd 

Cambridge University 

Cambridge, CB2 IEP 

ENGLAND 

Telephone: 0223 336450 

Michael H Frey 

JEOL USA INC 



Telephone: 617 535-5900

Alan Freyer 


6 Chahdlee Lab-Chemistry Dept 


Telephone: 814 865-0231 

Ethel From 

Mount Holyoke College 


South Hadley, MA 01075 

Telephone: 413 538-2349 

Eiichi Fukushima 

Lovelace Medical Foundation 

2425 Ridgecrest Drive, S.E. 

Albuquerque, NM 87108 

Telephone: 505 262-7155 

Bing M Fung 

Univ of Oklahoma 

Dept of Chem " 

Norman, OK 73019 

Telephone: 405 325-3092 

George T. Furst 


2505 33RD Street 


Telephone: 215 898-3407 

Michael M. Fuson 

Wabash College 

Crawfordsville, IN 47933 

Telephone: 317 364-4241 

Colin A. Fyfe 


Univ of British Columbia 

Vancouver, BC, V6T IY6 

CANADA 

Telephone: 604 228-2293 

Robert A. Gale 

M R Resources 



Telephone: 617 632-7000 

Kathleen S. Gallagher 

Univ of New Hampshire 

Parsons Hall 

Durham, NH 03824 

Telephone: 603 862-3597 

Michael Gamcsik 

Johns Hopkins Univ 

720 Rutland Ave. 


Telephone: 301 955-7491 

Xiaolian'Gao 

Columbia Univ; Dept of Biochem 

630 W 168th Street 


Telephone: 212 305-5280 

Albert R. Garber 

Univ of So Carolina 



Telephone: 803 777-2088 

Joel R Garbow 

Monsanto Co. 

700 Chesterfield Vill Pkwy 


Telephone: 314 537-6004 

Janice Koles Garde 

Monsanto Co. 

800 N. Lindberg Blvd. 


Telephone: 314 694-1172 

Dale R. Gardner 

Procter & Gamble 

6071 Center Hill Road 


Telephone: 513 659-4846 

Allen N. Garroway 


Code 6122 


Telephone: 202 767-2323 

Dr. Thomas Gedris 


Chemistry Dept. NMR Lab 

Tallahassee, FL 32306 

Telephone: 904 644-5586 

Leslie Gelbaum 

Georgia Tech 

Research Center for Biotech 


Telephone: 404 894-3700 

Dr. Walter V Gerasimowicz 


Code 6122, Chemistry Division 


Telephone: 202 767-2323 

B. C. Gerstein 

Iowa State University 

229 Spedding I SU 

Ames, IA 50011 

Telephone: 515 294-3375 

Henrik Gesmar 

HC Orsted Inst, Dept of Chem 

5, Universitetsparken 

DK-2100 Copenhagen, 

DENMARK 

Telephone: 1 35 31 33 X610 

Paul J Giammatteo 

Texaco Inc. 

PO Box 509 

Beacon, NY 12508 

Telephone: 914 831-3400 X6 

Atholl A. Gibson 

Nalorac Cryogenics Corp 

837 Arnold Drive, Suite 600 

Martinez, CA 94553 

Telephone: 415 229-3501 

Russell Gillis 

The Upjohn Company 

M/S 1140-230-2, 7171 Portage 

Kalamazoo, MI 49001 

Telephone: 616 323-5779 

T. E. Glass 

Virginia Tech 

Dept of Chem 


Telephone: 703 961-5385 

John Glushka 

The Rockefeller University 

1230 York Avenue, Box 299 


Telephone: 212 570-8269 

William Gmeiner 




Telephone: 801 581-3014

John Gobbi 

Dow Chemical; PO Box 3030 

Vidal St; AR&D, Bldq 63 

Sarnia/Ontario, N7T 7MI 

CANADA 

Telephone: 519 339-5221 

Wendy Goldberg 

Merck Isotopes 

PO Box 2000 Ry 33-50 


Telephone: 201 574-4207 

Oded Gonen 

MIT 

RM. 6-133 


Telephone: 617 253-2380 

Nina C. Gonnella 

CIBA GEIGY 

556 Morris Ave. 


Telephone: 201 277-7265 

Ricardo Gonzalez-Mendez 

Stanford Univ Sch of Medicine 

Department of Pediatrics, $214 

Stanford, CA 94305-5119 

Telephone: 415 723-5859 

Mary C Goodberlet 

Eastman Kodak 

B339 ATD 


Telephone: 716 722-3253 

Myra Gordon 

Isotec Inc 

3858 Benner Road 

Miamisburg, OH 45342 

Telephone: 800 448-9760 

Dr. David Gorenstein 

Purdue University 


West Lafayette, IN 47907 

Telephone: 317 494-7851 

Koji Goto 

Asahi Chemical Industry Amer 

350 Fifth Ave. Suite 7412 


Telephone: 212 695-6720 

David W Graden 

Janssen Res Foundation 

McKean & Welsh Rds 

Spring House. PA 19477 

Telephone: 215 628-5884 

Philip Grandinetti 

Univ of lllinois-Urbana 

505 S Mathews Box 48-I 


Telephone: 217 244-1140 

Anne Grant 

Hoffmann-LaRoche Inc 

340 Kingsland Street 

Nutley, NJ 07110 

Telephone: 201 235-5108 

David M. Grant 


1320 HEB, Chemistry Department 


Telephone: 801 581-8854 

Peter Grant 


611Hansen 

Palo Alto, 

~Y94303 

Telephone: 415 493-4000 

David Graves 


Univ. of Mississlppi 

University, MS 38677 

Telephone: 601 232-7732 

George Gray 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Dr Christian Griesinger 

ETH Zurich-Phy Chem Lab 

ETH Zentrum 

Zurich, 

CH-8092 SWITZERLAND 

Telephone: 01 256 4375 

Robert G. Griffin 

MIT 

NW14-5113, 77 Mass Avenue 


Telephone: 617 253-5597 

Bruce Griffith 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Stephen Grode 

The Upjohn Co. 

1140-230-2 


Telephone: 616 323-4316 

Terry W. Gullion 

Washlngton University 



Karl Gunderson 

Ciba-Geigy Corp. 

556 Morrls Avenue 


Telephone: 201 277-5285 

Fred Haberle 

Brucker Instruments 

Mannin 9 Park 


Telephone: 617 667-9580 

Myrna Hagedorn 

Int'l. Flavors & Fragrances 

1515 Highway 36 

Union Beach, NJ 07735 

Telephone: 201 264-4500 

Elisabeth Hajdu 

G.D. Searle & Co. 

4901Searle Parkway 


Telephone: 312 982-4675 

James E. Hall 

ICl Americas 

Concord Pike and Murphy Road 


Telephone: 302 575-8302 

~ e!en-Ne]l Hallada~. 

eton Mall university 

Chemistry South Orange Ave. 

South Orange. NJ 07079 

Telephone: 201 761-9029

Gordon Hamer 

Xerox Research Center-Canada 

2660 Speakman Drive 

Mississauga, Ont., L5K 2LI 

CANADA 

Telephone: 416 823-7091 

Philip K. Hammen 


Department of Chemistry, B6-I0 


Telephone: 206 545-2086 

Dr Charles F Hammer 

Georgetown University 



Telephone: 202 687-6170 

Terry E. Hammond 

B P America 

4440 Warrensville Road 


Telephone: 216 581-5929 

Ronald L. Haner 

University of California 


Santa Cruz, CA 95064 

Telephone: 408 429-4382 

Dr. Wayne Harris 

ICN Biomed Inc-Stable Isotopes 

3300 Hyland Avenue 

Costa Mesa, CA 92626 

Telephone: 714 545-0113 

Aidan T. Harrison 

Cornell University 

Dept of Chem, B-71 Baker Lab 

Ithaca, NY 14853-1301 

Telephone: 607 255-8548 

Arnold M. Harrison 

Union Carbide Tech Center 

P.O. Box 8361 

South Charleston, WV 25303 

Telephone: 304 747-5898 

J. Stephen Hartman 


Brock University 

St. Catharines, Ont., L2S 3AI 

CANADA 

Telephone: 416 688-5550 

Cynthia Hartzell 

Los Alamos National Lab 

P. O. Box 1663, LANL C345 

Los Alamos, NM 87545 

Telephone: 505 667-9806 

Syed Hasan 

Nutra Sweet 

601 East Kensington Road 

Mt. Prospect, IL 60056 

Telephone: 312 506-2376 

Andy Hasenfeld 




Telephone: 609 987-2901 

Galen R. Hatfield 

Allied-Signal 

Corporate Technology 

Morristown, NJ 07960 

Telephone: 201 455-2794 

Bruce Hawkins 

Colorado State University 



Telephone: 303 491-6455 

Sarah L. Heald 


333 Cedar Street, Box 3333 


Telephone: 215 785-4607 

Jerry Heeschen 

Dow Chemical Company 

Analytical Sciences 1897 

Midland, MI 48667 

Telephone: 517 636-5330 

Gregory J. Heffron 




Telephone: 315 423-1021 

Gregory L. Helms 

Univ of Hawaii-Dept of Chem 

2545 The Mall 

Honolulu, HI 96822 

Telephone: 808 948-6471 

Roseann Helms 


600 Clemson Rd. 


Telephone: 803 788-6497 

Janet M. Henderson 

Nabisco Brands Tech Ctr 

100 Deforest Avenue 

East Hanover, NJ 07936 

Telephone: 201-503-3418 

P. Mark Henrichs 

Eastman Kodak Co. 

FI. 2, B.81 


Telephone: 716 477-6229 

Griselda Hernandez 




Telephone: 716 275-8268 

J. Michael Hewitt 

Eastman Kodak 

B339 Kodak Park 


Telephone: 716 722-3208 

Robert Highet 

Natl Heart Lung & Blood Inst 

Bldg. 10, Rm. 7N320 


Telephone: 301 496-3237 

Howard Hill 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

David F. Hillenbrand 

OTS Inc 

46 Manning Road 


Telephone: 617 671-0811 

Bruce Hilton 

NCI-FCRF; Prog Resources Inc 

PO Box B, Bldg 469, Room 162 

Frederick, MD 21701 

Telephone: 301 694-1226

Tetsuo Hinomoto 

JEOL USA Inc 

11 Dearborn Rd. 


Telephone: 617 535-5900 

Robert C. Hirst 

Goodyear Tire & Rubber Co. 

142 Goodyear Blvd, 415A 

Akron, OH 44305 

Telephone: 216 796-9104 

Gina Hoatson 

College of William & Mary 

Physics Department 

Williamsburg. VA 23185 

Telephone: 804 253-4471 

Roy Hoffman 


NMR/Data Proc Lab, Bowne Hall 


Telephone: 315 423-1201 

Bruce R Hofman 

Wyeth-Ayerst 

CN 8000 


Telephone: 201 274-4335 

Wade G. Holcomb 

Yale Univ School of Medicine 

185 Linden St. 


Telephone: 203 785-5296 

Robert S. Honkonen 


11810 East Miami River Road 

Ross, OH 45061 

Telephone: 513 245-2959 

Joseph P. Hornak 

Rochester Inst. of Tech. 



Telephone: 716 475-2904 

Phil Hornung 




Telephone: 415 659-2600 

David I. Hoult 

.NIH, Bldg. 13 Room 3W13 

9000 RocEville Pike 


Telephone: 301 496-5771 

Grace Hsu 

M & T Chemicals 

PO Box 1104 


Telephone: 201 499-2177 

Victor L. Hsu 

Univ of Calif, San Diego 

Dept of Chemistry. B-042 

ta Jolla, CA 92093-0342 

Telephone: 619 534-4896 

Jianzhi Hu 

Wuhan Institute of Physics 

Wuhan, Post Office Box 241 

Wuhan, Hubei, 430071 

P. R. of China 

Telephone: 812 541-204 

Dee-Hua Huang 

Univ of Alabama 

NMR FacilitylCHSB B-31 

Birmingham, AL 35294 

Telephone: 205 934-5695 

Shaw Huang 

Harvard University 

12 Oxford Street 


Telephone: 617-495-3939 

Tai-huang Huang 

Georgia Inst of Tech 

School of Physics 


Telephone: 404 894-2821 

Donald W. Hughes 



Hamilton, Ont., LBS 4MI 

CANADA 

Telephone: 416 525-9140 

Stephen Huhn 

Nabisco Brands 

I00 DeForest Ave 


Telephone: 201 503-4719 

Ann H. Hunt 

Lilly Research Labs 

Dept. MC525 

Indianapolis, IN 46285 

Telephone: 317 276-4404 

Catherine T. Hunt 

Rohm & Haas Co 

727 Norristown Rd, B1dg 8B 


Telephone: 215 641-2035 

Robert W. G. Hunt 

10 Kewferry Road 

Northwood 

Middlesex, 

ENGLAND HA2 2NY 

Brian K. Hunter 

~ ueen's University 

ingston, Ontario, K7L 3N6 

CANADA 

Telephone: 613 545-2620 

Ralph Hurd 




Telephone: 415 683-4396 

Howard Hutchins 

JEOL USA INC 

11 Dearborn Rd .-- 

Peabody, MAO~960 

Telephone: 617 535-5900 

William C. Hutton 

Monsanto Co. BB3K 

lO0 Chesterfield Vill Pwy 


Telephone: 314 537-6021 

Yuying C. Hwang 

Washington Univ-Dept of Chem 

1Brookings Drive 


Telephone: 314 889-6583 

Sven G. Hyberts 

U of Mich-Biophy Res Division 

2200 Bonisteel Boulevard 

Ann Arbor, MI 48109 

Telephone: 313 936-3852

Timothy Hyman 




Telephone: 315 423-1021 

Geno lannaccone 

VPI & SU 



Telephone: 703 961-6578 

Paul T. Inglefield 


Clark Universi~{610 

Worcester, MA 

Telephone: 617 793-7653 

Ruth R. Inners 


Mannin 9 Park 


Telephone: 617 667-9580 

Dan Iverson 


611 Hansen 

Palo Alto, W~Y94303-0883 

Telephone: 415 493-4000 

Pradeep Iyer 

UNOCAL 

376 South Valencia Avenue 

Brea, CA 92621 

Telephone: 71452872011432 

Cynthia Jackson 

Univ. of Rochester 



Telephone: 716 275-8268 

Victoria Jacob 

Spectral Data Services, Inc. 

818 Pioneer 

Champaign, IL 61820 

Telephone: 217 352-7084 

Nazim J. Jaffer 

Dept. of Chemistry & Biochem 

UCLA 

Los Angeles, CA 90024 

Telephone: 213 825-1816 

Nathan Janes 

Thomas Jefferson University 

11th & Walnut St-Pavillion 405 


Telephone: 215 928-5022 

Norma Jardetzky 

SMRL, 5055 Lomita Drive 


Stanford, CA 94305-5055 

Telephone: 415 723-6270 

Linda A. Jelicks 

Albert Einstein Col Med/Biophy 

1300 Morris Park Ave, Bldg U 

Bronx, NY 10461 

Telephone: 212 430-3591 

Lynn W. Jelinski 

AT&T Bell Laboratories 

600 Mountain Ave. 


Telephone: 201 582-2511 

Gary L. Jewett 

Dow Chemical 

1897 Building 


Telephone: 517 636-4694 

Yi Jin Jiang 

Univ of Utah 



Telephone: 801 581-7351 

Boban K. John 




Telephone: 415 683-4358 

Bruce A. Johnson 


Dept of Mol Biophys PO 3333 


Telephone: 203 785-4605 

Connie Johnson 


Manning Park 

Billerica,.MA 01821 

Telephone: 617 667-9580 

James H. Johnson 

Hoffmann-La Roche 

340 Kingsland St./Bldg. 71 

Nutley, NJ 07110 

Telephone: 201 235-2415 

LeRoy Johnson 




Telephone: 415 683-4410 

Michael E. Johnson 

Univ of Ill Med Chem Dept 

M/C 781, P. O. Box 6998 

Chicago, IL 60680 

Telephone: 312 996-0796 

Robert D. Johnson 

IBM Almaden Research 

650 Harry Road 

San Jose, CA 95120 

Telephone: 408 927-1661 

Eric R. Johnston 

Haverford College 


Haverford, PA 19041 

Telephone: 215 896-1216 

Jiri Jonas 

Univ of Illinois, Chem Dept 

1209 W. California 


Telephone: 217 333-2572 

Claude R Jones 

Purdue Univ. 


W. Lafayette..IN 47907 

Telephone: 317 494-5287 

Paul-James Jones 




Telephone: 203 432-3992 

Robert L. Jones 

Emory Univ~ Chem Dept 

1515 Pierce Dr 


Telephone: 404 727-6621

F 

Andrew Joseph 

Phospho-Ener~etics 

2 Raymond Drive . 

Havertown, PA 19083 

Telephone: 215 789-7474 

Beat Jucker 




Telephone: 315 423-1021 

Gary P juneau 

Olin Corp 

350 Knotter Dr PO Box 586 

CheShire, CT 06410-0586 

Telephone: 203 271-4~2 

Alicia D. Kahle 

E.R. Squibb& Sons 

PO Box 4000 

Princeton~ NJ 08540 

Telephone: 609 921-4992 

Matthew W Kalnik 


630 W 168th St; P&S 3-444 


Telephone: 212 305-5280 

Lou-Sing Kan 

Johns Hopkins University 

615 North Wolfe Street 


Telephone: 301 955-2043 

Rasesh Kapadia 

Case Western Reserve Univ 

Univ Circle; Dept of Chem 


Telephone: 216 368-2636 

David B. Kaplan 

Pittsburgh NMR Institute 



Telephone: 412 647-6674 

Samuel Kaplan 

Xerox Webster Res Center 

800 Phillips Rd../S 24-0 

Webster, NY 14580 

Telephone: 716 422-4784 

Leela Kar 

Univ of I11inois at Chicago 

Dept of Med Chem. Box 6998 


Telephone: 312.996-5278 

Rodney V. Kastrup 

Exxon Research & Engineering 

Rte. 22 E. Clinton Township 

Annandale, NJ 08801 

Telephone: 201 730-2117 

Larry Kasuboski 

Georgetown Univ Hosp Radiology 

3800 Reservoir Road, NW 


Telephone: 202 784-3359 

Roger Kautz 

Yale M. B. & B. 

260 Whitney Avenue, POBox 6666 

New Haven, CT 0651t 

Telephone: 203 432-5649 

Lewis E. Kay 




Telephone: 203 432-3937 

Paul A. Keifer 

School of Chem. Sci. Box 95-9 

Univ. of Illinois 


Telephone: 217 333-2041 

Toni Keller 


Mannin~ Park 


Telephone: 617 667-9580 

M. F. Kelly 

Kodak Limited 

Research W92 Headstone Drive 

Harrow, Middlesex, HA1 4TY 

U.K. 

Telephone: 441427438033198 

Michael F. Kelly 


2S5 Fourier Avenue 


Telephone: 415 683-4419 

Larry Kelts 

Eastman Kodak Co 

Research Laboratories Bldg 82 


Telephone: 716 722-9121 

Raymond Kendrick 

IBM 


San Jose, CA 95120-6099 

Telephone: 408 927-2455 

Gordon J. Kennedy 

Union Carbide Co. 

PO Box 670 

Bound Brook, NJ 08805 

Telephone: 201 563-5074 

Michael A. Kennedy 


Dept of Chemistry, 621 Main St 


Telephone: 803 777-7399 

Scott Kennedy 

Univ. of Rochester 

601Elmwood Avenue 


Telephone: 716 275-8268 

Bill Kenney 


611Hansen Way 


Telephone: 415 493-4000 

Kenneth Keymel 


ATD Bldg-339; 1669 Lake Ave 


Telephone: 716 722-3218 

Mohammad A Khadim 

Hoechst Celanese Corp 

SOD Washington Street 

Coventry, RI 02816 

Telephone: 401 823-2111 

Roy W. King 




Telephone: 904 342-0592

Robert A Kinsey 

BF Goodrich 

9921Brecksville Road 

Brecksville, OH 44141 

Telephone: 216 447-5317 

Ernest Kirkwood 

John Wiley & Sons 

Baffins Lane 

Chichester, Sussex, 

ENGLAND P019 IUD 

Telephone: 01 44 243770303 

Hans J Koch 

MSD Isotopes 

PO Box 899; Pte-Claire 

Dorval, Quebec, HgR 4P7 

CANADA 

Telephone: 514 695-7920 

Frank Koehn 

Harbor Branch Oceanogr. Inst. 

5600 Old Dixie Highway 

Ft. Pierce, FL 34946 

Telephone: 305 465-2400 

Susan Kohler 

HMS NMR Lab 

221Longwood Ave. 


Telephone: 617 732 1377 

Andrew C. Kolbert 

MIT, Francis Bitter Mag Lab 



Telephone: 617 253-0462 

Marvin Kontney 

Univ of Wisconsin 



Telephone: 608 262-0563 

Alan M. Kook 

Rice University 

Dept. Chemistry/Rm. 309 


Telephone: 713 527-8101 

Kenneth D. Kopple 

Smith Kline French Labs 

P.O. Box 1539 

King of Prussia, PA 19406 

Telephone: 215 270-6659 

Donald W. Kormos 

Case Western - University Hosp 

2074 Abington Rd, Dept/Radiolg 

Cleveland, ON 44106 

Telephone: 216 844-7750 

L. S. Kotlyar 

Natl Research Coun of Canada 

Ottawa, Ontario, KIA OR6 

CANADA 

Telephone: 613 993-2011 

Michael Kouchakdjian 


630 W 1681h St 


Telephone: 212 305-5280 

Thomas Krick 

University of Minnesota 

1479 Gortner Avenue 

St. Paul, MN 55108 

Telephone: 612 624-7715 

Richard Kriwacki 

Boehringer Ingelheim Ltd. 

90 E. Ridge Rd. 

Ridgefield, CT 06877 

Telephone: 203 798-5184 

Thomas R. Krugh 




Telephone: 716 275-4224 

Katsuhiko Kushida 


611Hansen Way 


Telephone: 415 493-4000 

David Kwoh 

International Paper 

Long Meadow Road 

Tuxedo, NY 10987 

Telephone: 914 577-7413 

Laurine A. LaP1anche 

Northern Illinois University 


DeKalb, IL 60115 

Telephone: 815 753-6873 

Steven R. LaPlante 


306c Bowne Hall 


Telephone: 315 423-1021 

Serge Lacelle 

Universite de Sherbrooke 

Department Chimie 


CANADA 

Telephone: 819 821-7823 

Joseph B. Lambert 


Northwestern University 

Evanston, IL 60208 

Telephone: 312 491-5437 

Lisa Lambert 


611Hansen Way 


Telephone: 415 493-4000 

David Lankin 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

James Lappegaard 

Chemagnetics Inc 

43 Lenape Trail 

Denville, NJ 07834 

Telephone: 201 627-8875 

Joseph Laughlin 


Mannin~ Park 


Telephone: 617 667-9580 

Frank Laukien 


Manning Park 


Telephone: 617 667-9580 

Paul C. Lauterbur 


1307 West Park Street 


Telephone: 217 244-0600

W. John Layton 

Univ of Kentucky 

Mag Res Ctr, 101 Stone Bldg 

Lexington, KY 40506-0053 

Telephone: 606 233-8993 

Juliette T. Lecomte 


Chem Dept, 152 Davey Lab 


Telephone: 814 863-1153 

Carolyn Lee 

MIT, Natl Magnet Lab 

Rm NW14-5119. 170 Albany St. 


Telephone: 617 253-0484 

Chang J. Lee 




Telephone: 609 987-2901 

Cheol E. Lee 


230 S. 34th St.. Oept of Chem 


Telephone: 215 898-8732 

Hee Cheon Lee 

U. of Ill at Urbana-Champaign 

Box 23-1, 505 S. Mathews 


Telephone: 217 333-8328 

Jonathan P. Lee 

Harvard Medical School 

185 Pilgrim Road 


Telephone: 617 732-9501 

Joseph H.C. Lee 

Southern Illinois Univ 

Oept of Chem & Biochem 

Carbondale, IL 62901 

Telephone: 618 453-5721 

Suzannie C. Lee 

Proctor & Gamble Co. 

Miami Valley Labs, Box 398707 

Cincinnati, OH 45239-8707 

Telephone: 513 245-2551 

Yang-Chih Lee 

Thomas Jefferson University 

DeptlPath, JAH Hall, Room 239 


Telephone: 215 928-7883 

Yu-Hwei Lee 

Univ Illinois 

Med Chem Dept. Rm 544, m/c781 


Telephone: 312 996-5278 

Mark Leifer 




Telephone: 415 659-2600 

William C Lenhart 


ATSD B339 Kodak Park 


Telephone: 716 722-3238 

Gregory Leo 

Monsanto Agricultural Co 

800 N. Lindbergh Blvd., U3E 


Telephone: 314 694-5629 

Mary Frances Leopold 




Telephone: 801 581-7351 

Charles L. Lerman 

ICI Americas 

Concord Pike & Murphy Road 


Telephone: 302 575-2577 

Laura Lerner 

NIH 

Bldg 2 Pan B2-08, LCP,NIDDK 


Telephone: 301 496-2704 

Cathy Lester 


Chem Dept, Hutchinson Hall 


Telephone: 716 275-8268 

John R. Levine 

GE NMR Instrument 



Telephone: 415 683-4408 

George.C. Levy 

Chemlscry uept. 



Telephone: 315 423-1021 

Barbara A. Lewis 




Telephone: 608 262-1563 

Tom Lewis 


611Hansen Way 

Palo Alto, CA'94303 

Telephone: 415 493-4000 

Robert L. Lichter 

Suny-Stony Brook 

2401 Lab Office Bldg 

Stony Brook, NY I1794-4433 

Telephone: 516 632-7035 

Fu-Mei Lin 

Calgon Corp 

PO Box 1346 


Telephone: 412 777-8597 

Fu-Tyan Lin 

Univ of Pittsburgh 

1305 CB/Chem. Dept. 


Telephone: 412 624-8403 

Andrew S. Lipton 


305 Bowne Hall-Oept of Chem 


Telephone: 315 423-1021 

Mark Lisicki 




Telephone: 412 268-3411

Jay J. Listinsky 

U of Rochester-Dept of Radlgy 

Box 648-601E'lmwood-Strong Mem 


Telephone: 716 235-5541 

Guoying Liu 


Box 23 NL, 505 S. Mathews Ave. 


Telephone: 217 333-3897 

David Live 

Emory University 



Telephone: 404 727-0867 

Carol Loeschorn 

ICN Biomed Inc-Stable Isotopes 

3300 Hyland Avenue 

Costa Mesa, CA 92626 

Telephone: 714 545-0113 

Timothy M. Logan 

University of Chicago 

5735 S. Ellis Ave. 


Telephone: 312 702-3456 

Robert C Long Jr 

Emory Univ; Dept of Chem 

1515 Pierce Dr 


Telephone: 404 727-6589 

Jan Lovy 

Kingston Technologies Inc 

2235-B Route 130 

Dayton, NJ 08810 

Telephone: 201 274-2288 

Linda A Luck 


University of Vermont 

Burlington, VT 05405 

Telephone: 802 656-3461 

Barbara A. Lyons 


1112 E. State . 

Ithaca, NY 14853 

Telephone: 607-255-4784 

Dr. Peter M. MacDonald 

Harvard Medical School 



Telephone: 617 732-9501 

Prof Gary E. Maciel 




Telephone: 303 491-6480 

James W. Mack 

Nat Inst of Health 

Building 10 Room 12N238 


Telephone: 301 496-7193 

Albert Macorski 


Dept of Elect Eng, Durand Bldg 


Telephone: 415 723-2708 

Alexander Macur 

New Methods Research Inc 

719 East Genesee St. 


Telephone: 315 424-0329 

Paul D. Majors 

Lovelace Medical Foundation 

2425 Ridgecrest Drive, S.E. 


Telephone: 505 262-7155 

J. Anthony Malikayil 

Dept. MBB, 333 Cedar St. 

Yale Univ. 


James J. Maloney 

ICI Americas Inc 

Concord Pike and Murphy Road 


Telephone: 302 575-8545 

Suraj P Manrao 

Merck & Co., Isotopes 

PO Box 2000, R33-210 


Telephone: 201 574-6980 

Kirk Marat 

University of Manitoba 


Winnipeg, Manitoba, R3T 2N2 

CANADA 

Telephone: 204 474-6259 

Paul S. Marchetti 

AKZO Chemicals, Inc. 

Livingstone Avenue 

Dobbs Ferry, NY 10522 

Telephone: 914 693-1200 

Joseph J Marcinko 




Telephone: 216 368-2636 

Thomas H. Mareci 


Dept of Radiology. Box J-374 


Telephone: 904 395-0293 

Martin Marek 


611Hansen 

Palo Alto, 

~Y94303-0883 

Telephone: 415 493-4000 

Guenter G. Maresch 


650 Harry Rd., K321802 


Telephone: 408 924-2916 

Dominique Marion 

MIDDK - Lab of Chem Physics 

Rockville Pike 


Telephone: 301 496-2706 

John L. Markley 


Dept of Biochem-420 Henry Mall 


Telephone: 608 263-9349 

Brian J Marsden 

Natl Res Council of Canada 

100 Sussex Dr 

Ottawa, KIA OR6 

CANADA 

Telephone: 603 990-0837

Eric A'. Marshall 

U~ of Rochester-Dept of Biophy 

Rochester Medical Center 


Telephone: 716 275-8268 

Joel F. Martin " 

Dept. of Radiology/H-756 

UniV. of Calif.-San Diego 


Telephone: 619 543-2953 

G. D. Mateescu 

Chem Dept, 2074 Adelbert Rd 


Clev@land, OH 44106-2699 

Telephone: 216 368-2589 

Shigeru Matsui 

Oept of Chemistr~ 

Univ of Californla 


Telephone: 415 642-2094 

Mark Mattingly 


Mannin~ Park 

Billerlca, HA 01821 

Telephone: 617 667-9580 

Anabela Maynard 

Univ. of Toronto 

80 St. George St. 

Toronto, M55 IAI 

CANADA 

Telephone: 416 978-5728 

CharlesoL~.Ma~ne 

Dept. Ot ~nemlstry BI03 HEB 

Univ of Utah 

Salt Lake City UT 84112 

Telephone: 801 581-7413 

Tony Mazzeo 




Telephone: 315 423-1021 

Gene Mazzola 

Food & Drug Administration 

200 C. Street, SW - (HFF-423) 


Telephone: 202 245-1409 

James D. McCurry 




Telephone: 215.758-3480 

Paula L. McDaniel 

Box 35-I Dept. of Chemistry 

Univ. of Illinois 


Telephone: 217 333-3581 

Ann E. McDermott 

MIT, Francis Bitter Mag Lab 

170 Albany Street, NW14-5107 


Telephone: 617 253-5586 

Douglas McFaddin 

CANMET - Ergy Mines & Resource 

555 Booth Street 

Ottawa, Ontario, KIA OGI 

CANADA 

Telephone: 613 995-0296 

William McGranahan 

JEOL USA INC 



Telephone: 617 535-5900 

Robert A. McKay 

Chem Dept, I Brookings Dr. 



Telephone: 313 889-6617 

Michael S. McKinnon 

DuPont Canada 

Research Center PO Box 5000 

Kingston, Ont., K7L 5A5 

CANADA 

Telephone: 613 544-6400 

Ian J. McLennan 

John Hopkins Medical School 

Dept. of Radiology 


Telephone: 301 955-7491 

Ronald McNamara 

Dept. of Chem., 231S 34th St 


Philadelphia, PA 19104-6323 

Telephone: 215 898-4886 

Michael D. Meadows 

Dow Chemical 

Bldg B-1219 

Freeport, TX 77546 

Telephone: 409 238-1644 

James H Medley 

Bristol-Myers Co. 

PO Box 4755 


Telephone: 315 432-2410 

Elizabeth MeW 

FSIS 

308-D Lansdale Ave. 

Millbrae, CA 94030 

James D. Meinhart 

Chem. Dept., 5735 S. Ellis Ave 

Univ of Chicago 


Telephone: 312 702-3456 

Michael T Melchior 

Exxon Research 

Clinton Township, Route 22 E 


Telephone: 201 730-2114 

Ronald A. Merrill 

Sun Refining & Marketing Co 

PO Box 1135 

Marcus Hook, PA 19063 

Telephone: 215-447-1743 

David V. Mesaros 

DuPont Co. 

Experimental Station 


Telephone: 302 695-7398 

Kenneth R. Metz 

New England Deaconess Hospital 



Telephone: 617 732-8460 

Frank Michaels 

Eastman Kodak 

66 Eastman Avenue 


Telephone: 716 722-140g

Dale Mierke 

Univ of Calif, San Diego 

Chemistry Dept B-OI4 


Telephone: 619 534-2594 

John M. Millar 


Dept of Chem, P. O. Box 6666 


Telephone: 203 432-3933 

Joel B Miller 

Naval Research Lab 

Code 6120 


Telephone: 202 767-2337 

• Bill Millman 

Univ of Wisconsin-Milwaukee 

Dept of Chem, P. O. Box 413 


Telephone: 414 229-5310 

Virginia Miner 

Dow Chemical Co 

1897 Building 


Telephone: 517 636-5321 

Jan Mintorovitch 

University of New Mexico 



Telephone: 505 277-2060 

Prasanna K. Mishra 




Telephone: 412 268-3161 

Gaetano Montelione 

University of Michigan 



Telephone: 313 936-3851 

Ed Mooberry 




Telephone: 608 263-9493 

Sandra Mooibrock 


Mannin 9 Park 


Telephone: 617 667-9580 

J. Robert Mooney 

B.,P. America 

4440 Warrensville Center Road 


Telephone: 216 581-5824 

Kim Moore 


Mannin 9 Park 


Telephone: 617 667-9580 

C. Morat 

Carleton University 


Ottawa, Ontario, KIS 5B6 

CANADA 

Telephone: 613 564-6623 

Fred Morin 

1349 Larose Ave. 

Ottawa, Ont., KIZ 7X4 

CANADA 

Telephone: 613 729-5865 

Doug Morris 




Telephone: 803 777-7399 

Mark R. Mowery 

Central Michigan Univ/MMI 

1910 West St. Andrews Road 


Telephone: 517 832-5555 

Foad Mozaxeni 

Akzo Chemle America 

8401W. 47th St. 

McCook, IL 60525 

Telephone: 312 442-7100 

Karl T. Mueller 

Univ of California at Berkeley 



Telephone: 415 486-4875 

Luciano Mueller 

Smith Kline & French Labs 


King of Prussia, PA 19406-0939 

Telephone: 215 270-6658 

Detlev Muller 


Manning Park 


Telephone: 617 667-9580 

Michael Munowitz 

Amoco Research Center 

P.O. Box 400 


Telephone: 312 961-7844 

Sandra Murawski 


11520 Reed Hartman Highway 


Telephone: 513 530-3749 

Michael Murphy 




Telephone: 215-898-8732 

Paul Murphy 

IBM ISTG HPA 

B/630 Z/E70 D/12W 

Hopewell Junction, HY 12151 

Telephone: 914 892-2237 

Joseph Murphy-Boesch 

Fox Chase Cancer Ctr 

AOH/NMR Lab; 7701Burholme Ave 


Telephone: 215 728-3156 

Martin S Mutter 

Janssen Res Foundation 

McKean & Welsh 

Spring House. PA 19477-0776 

Telephone: 215 628-5538 

Barbara L. Myers-Acosta 

Lockheed Missiles & Space Co. 


Sunnyvale, CA 94088-3504 

Telephone: 408 756-3234

Kuniaki Nakagama 

JEOL Biometrology Lab 

Nakagami Akishima 

Tokyo 196, 

JAPAN 

Vitas Narutis 

Nalco Chemicals 

One Nalco Center 


Telephone: 321 961-9500 

Gil Navon 

NIH 

Bldg. 10, Room BID-138 


Telephone: 301 496-8139 

Thomas G. Neiss 

Dept. of Chem. Mudd Bldg. #6 

Lehigh Universit 

Bethlehem, PA 18~15 

Telephone: 215 758-3480 

Janis T. Nelson 

Syntex Research 

3401Hillview Ave., R6-002 


Telephone: 415 855-5649 

Sarah J. Nelson 


7701Burholme Avenue 


Telephone: 215 728-3561 

Gregory Nemeth 

Northwestern Univ Chem Oept 

2145 Sheridan Road 

Evanston, IL 60201 

Telephone: 312 491-7080 

Richard D. Newmark 

Lawrence Berkeley Lab-U of Cal 

MS 55-121, 1 Cyclotron Road 


Telephone: 415 486-4433 

Feng Ni 


Dept of Chem, 164 Baker Lab 


Telephone: 607 255-4737 

Linda K. Nicholson 


Institute of Molecular Biophys 


Telephone: 904 644-3254 

Niels Chr. Nielsen 

Dept of Chem 

Univ of Aarhus 

DK-800O Aarhus, 

DENMARK 


Walter P. Niemczura 

Univ of Hawaii-Dept of Chem 

2545 The Mall 

Honolulu, HI 96822 

Telephone: 808 948-7503 

N.R. Nirmala 

University of Michigan 

Biophy Res Div-2200 Bonisteel 


Telephone: 313 936-3852 

Robin A Nissan 

Naval Weapons Center 

Code 3851Michelson Lab 

China Lake, CA 93555 

Telephone: 619 939-1620 

Christopher North 

FL St U-Inst. Molecular Biophy 

1636 Jackson Bluff, #147 


Telephone: 904 644-3254 

Maureen P. O'Brien 


Dept of Chem. 225 Prospect St. 


Telephone: 203 432-3937 

Daniel J. O'Donnell 

Phillips Petroleum Company 

148 PL-PRC 

Bartlesville, OK 74004 

Telephone: 918 661-9776 

John F. O'Gara 

General Motors Res Labs 

30500 Mound Road, Oept 22 

Warren, MI 48090 

Telephone: 313 986-0833 

Mark O'Neil-Johnson 


Manning Park 


Telephone: 617 667-9580 

Byung Ha Oh 




Telephone: 608 262-4687 

Alan Olson 


3164 Ludlow Rd. 

Shaker Heights, OH 44120-2860 

Telephone: 216 991-7480 

Diana Omecinsky 

Parke Davis 

2800 Plymouth Rd 


Telephone: 313 996-7408 

Stanley J. Opella 




Telephone: 215 898-6459 

Anita M. Orendt 


Chemistry Dept, Box 69 


Telephone: 801 581-6116 

C. E. Osborne 

Tennessee Eastman Co 

Kingsport, TN 37662 

Telephone: 615 229-3413 

Gottfried Otting 

Inst fur Molec BiD und Biophys 

ETH-Honggerberg 

8093 Zurich, 

SWITZERLAND 


Jim Otvos 




Telephone: 414 229-5220

Jeanne C Owens 

Chemistry Dept., '.18-085 

Mass Inst of Technology 


Telephone: 617 253-0873 

Anthony Parker 

Libbey Owens Ford Company 

1701 East Broadway 

Toledo, OH 43605 

Telephone: 419 247-4258 

Victor Parziale 

Dynachem Corp. 

2631Michelle Dr 

Tustin, CA 92680 

Telephone: 714 730-4395 

Peter J Paterson 

JEOL USA INC 

11 Dearborn Rd 


Telephone: 617 535-5900 

Steven L. Patt 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 424-5696 

Sam Patz 

Brigham & Women's Hospital 

75 Francis Street 


Telephone: 6177325500x1444 

John Paxton 




Telephone: 415 659-2600 

Dan I. Pazara 


Chem Dept, University Circle 


Telephone: 216 368-5917 

Gerald A. Pearson 

Univ of Iowa 

Chem Dept 


Telephone: 319 335-1332 

John G. Pearson 




Telephone: 415 642-2094 

Thomas G. Perkins 




Telephone: 415 683-4383 

Marion Perpick-Dumont 

Univ of Toronto, Dept of Chem 

6 Ashmount Cresent 

Weston, Ontario, MgR IC7 

CANADA 

Telephone: 416 978-5728 

Richard Perry 

MSD Isotopes 

PO Box 899; Pte-Claire 

Dorval, Quebec, H9R 4P7 

CANADA 

Telephone: 514 695-7920 

Matthew Petersheim 

Seton Hall University 

Chem Dept, South Orange Avenue 

South Orange, NJ 07079 

Telephone: 201 761-9029 

Peter A Petillo 

Oept of Chem; Univ of WI 

II01Univ Ave 


Telephone: 608 273-0238 

Michael Petrel 

Arco Chemical Company 

3801 West Chester Pike 

Newtown, PA 19073 

Telephone: 215 359-2038 

Andrew M. Petros 


P. O. Box 1539, Mail Code L940 


Telephone: 215 270-5230 

Stephen B. Philson 

Univ of Minnesota 

207 Pleasant Street SE 

Minneapolis, MN 55455 

Telephone: 612 625-8374 

Francis Picart 

The Rockefeller University 

128 Peterson Street 

Brentwood, NY 11717 

Telephone: 212 570-8269 

Charles F. Pictroski 

Exxon Research & Engineering 

Clinton Twnshp, Rte 22 East 


Telephone: 201 730-2158 

Phil Pitner 

Boehringer Ingelheim 

90 E. Ridge 

Ridgefield, CT 06877 

Telephone: 203 798-5182 

Steven Pitzenberger 

Merck & Co. 

WP 26-100 

West Point, PA 19486 

Telephone: 215 661-7609 

Dan Plant 




Telephone: 415 

Nick Plavac 

Chem. Dept., 80 St George St 

University of Toronto 

Toronto, Ont., M5S IAI 

CANADA 

Telephone: 416 978-5728 - 

Emily Pleau 

Industrial Labs B. 339 



Mark D Poliks 

Washington Univ; Dept of Chem 

Box 1134 

St Louis, MO 63130 

Telephone: 314 889-5780 

C D Poon 

University of Oklahoma 


Norman, OK 73019 

Telephone: 405 325-3092

P~ 

/ 

Michael A Porubcan 

Squibb Inst for Medical Res 

PO Box 4000 


Telephone: 609 921-4991 

James H. Prestegard 


Chemistry Department, Box 6666 


Telephone: 203 432-5162 

Dr Caroline Preston 

Pacific Forestry Centre 

506 West Burnside Road 

Victoria, Brit Colum, VSZ IM5 

CANADA 

Telephone: 604 388-0720 

Elton Price 

Howard University 

525 College Street, N.W. 


Telephone: 202 636-6913 

Dr. K. O. Prins 

U of Amsterdam, Van der Waals 

VALCKENIERSTR. 67 

Amsterdam, I018XE 


Telephone: 020 525-6336 

Mohindar S. Puar 

Schering Corp 

60 Orange Street 

Bloomfield, NJ 07003 

Telephone: 201 429-3990 

Dr. Ronald J Pugmire 




Telephone: 801 581-7236 

David E Purdy 


R&D 186 Wood Ave South 


Telephone: 201 632-2894 

Enrico O. Purisima 

Biotech Rs Inst, NRC 

6100 Royalmount Ave 

Montreal, Que., H4P 2R2 

CANADA 

Telephone: 514-496-6343 

Gregory Quinting 

Sherwin-Williams Company 

10909 South Cottage Grove Road 


Telephone: 312 821-2167 

Dallas L. Rabenstein 



Riverside, CA 92521 

Telephone: 714 787-3585 

Tom Raidy 



Fremont, CA.94539 

Telephone: 415-683-4341 

S. Sunder Rajan 

Georgetown University Hospital 

Dept/Rad-3800 Reservoir Road 


Telephone: 202 784-2885 

Dr Vasanthan Rajanayagam 

Albert Einstein College of Med 

U 921, 1300 Morris Park Avenue 

Bronx, NY 10461 

Telephone: 212 430-2186 

Daniel P Raleigh 

MIT/Room NW 14-5107 

77 Mass. Ave. 


Telephone: 617 253-5586 

Preetha Ram 


Chem Dept-225 Prospect Street 


Telephone: 203 432-3992 

K. V. Ramanathan 




Telephone: 215 898-4886 

S. Ramaprasad 

3000 July Street, No. I08 


Stephen J. Rapposelli 

Wilmad Glass Co, Inc. 

Rte. 40 & Oak Rd. 


Telephone: 609 697-3000 

Mary Rastall 

Fiberglass Canada 

Technlcal Ctr, Box 3049 

Sarnia, Ontario, N7T 7X4 

CANADA 

Telephone: 519 336-5670 

C.I. Ratcliffe 

Natl Research Coun. of Canada 


CANADA 

Telephone: 613 993:2011 

Alan Rath 




Telephone: 415 659-2619 

Betty Rather 

Pennwalt Corp. 

900 First Street 

King of Prussia, PA 19406 

Telephone: 215 337-6614 

Bruce David Ray 

IUPUI Physics Dept 

PO Box 647 

Indianapolis, IN 46223 

Telephone: 317 264-6914 

G. Joseph Ray 

Amoco Corp. 

Amoco Res. Ctr., PO Box 400 


Telephone: 312 420-5217 

David B. Reader 




Telephone: 617 938-0067 

Robert A. Reamer 

Merck & Co. 

PO Box 2000, Bldg 801-210 

Rahway, NJ 07065-0900 

Telephone: 201 574-5391

Gade S. Reddy 


E328/161A 


Telephone: 302 695-3116 

Richard D. Redfearn 

DuPont 

FPD Research, 2571Fite Rd 

Memphis, Tn 38127 

Telephone: 901 353-7100 

Dr. Peter D. Regan 

Shell Research Ltd. 

Sittingbourne Research Centre 

Sittingbourne, Kent, 

MEg 8AG U.K. 

Telephone: 795-412-377 

Cindy M Reidsema 

IBM Corp; Dept T43/B1dg 257-2A 

1701 North Street 

Endicott, NY 13790 

Telephone: 607 757-1432 

Michael D. Reily 

Univ of Wisconsin - Madison 

Dept of Chem - 420 Henry Mall 


Telephone: 608 262-4687 

Nicholas V. Reo 

Wright St Univ, Cox Institute 

3525 Southern Boulevard 

Kettering, OH 45429 

Telephone: 513 299-7204 

Linda Reven 


1004 West Stoughton, Apt. 4 


Telephone: 217-333-8328 

William F. Reynolds 

Univ of Toronto 


Toronto, Ont., M5S IAI 

CANADA 

Telephone: 416 978-3563 

John Rieger 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Erro11S Riewerts 

Southwest Research Institute 

P.O. Box 28510 

San Antonio, TX 78284 

Telephone: 512 522-2735 

Peter Rinaldi 


The University of Akron 


Telephone: 216 375-5184 

James M. Riordan 

Southern Research Institute 

2000 9th Ave So, PO Box 55305 

Birmingham, AL 35255-5305 

Telephone: 205 581-2450 

William M Ritchey 


Case Western Reserve Univ. 


Telephone: 216 368-3668 

Jan Robert 

Lehigh Uni • Dept of Chem 

Mudd Bldg 


Telephone: 215 758-3480 

James E. Roberts 


Chem. Dept./Bldg. 6 


Telephone: 215 758-4841 

Pamela Roberts 


66 Eastman Ave 


Telephone: 706 477-5175 

Valerie Robinson 

Syntex Inc 

2100 Synte× Ct 

Mississauga, Ont., LSN 3X4 

CANADA 

Telephone: 416 821-4000 

Thomas S. Robison 

3M Company, Riker Laboratories 

3M Center, Bldg. 270-4S-02 


Telephone: 612 733-0702 

Ronald K. Rodebaugh 

Ciba Geigy Corp. 

444 Saw Mil| River Rd. 

Ardsley, NY 10502-2699 

Telephone: 914 478-3131 

Charles Rodger 

Bruker Spectrospin Canada 

555 Steeles Ave. East 

Milton, Ontario, LgT IY6 

CANADA 

Telephone: 416 876-4641 

Peter B. Roemer 

GE Corp Res & Development Ctr 


Schenectady, NY 12301 

Telephone: 518 387-5886 

Alan Ronemus 

Union Carbide Corporation 


South Charleston, WV 25303 

Telephone: 304 747-3651 

Mark S. Roos 

U of Cal-Lawrence Berkeley Lab 

MS 55-121, 1 Cyclotron Road 


Telephone: 415 486-4063 

Richard Rosanske 

Florida State Univ. 



Telephone: 904 644-5586 

Scott A Ross 

Calif Inst of Technology 

Mail Code 127-72 Caltech 

Pasadena, CA 91125 

Telephone: 818 356-6553 

David Ruben 

MIT, National Magnet Lab 



Telephone: 617 253-5598 

Dr. G. S. Rule 


Dept of Chem 


Telephone: 415 723-4576

~L 

Anne F. Russell 

Procter & Gamble, MV Labs 

PO Box 398707 

Cincinnati, OH 45239-8707 

Telephone: 513 245-2613 

Venceslav Rutar 


Chem Oept, 85H Gilman Hall 


Telephone: 515 294-5958 

Dr. Aaron C. Rutenberg 

Martin Marietta Energy Systems 

Bldg 9995, Y-12 Plant 

Oak Ridge, TN 37831 

Telephone: 615 574-241i 

Robert Rycyna 


Chemistry Department, Box 6666 


Telephone: 203 432-5208 

Timothy Saarinen 


Box 294 Baker Lab, Dept/Chem 

Ithaca, NY 14853-1301 

Telephone: 607 255-4980 

Ronald Sager 

Quantum Design 

11578 Sorrento Valley Rd Ste30 


Telephone: 619 481-4400 

Andre Saint-Jean 


Blvd Universite 


CANADA 

Telephone: 819 821-3099 

Felix Salines 

Univ of Texas Medical Branch 

200 University Blvd, Suite 601 

Galveston, TX 77550 

Telephone: 409 761-2360 

Ago Samoson 




Telephone: 415 642-1220 

Bryan C. Sanctuary 

McGill University 

Dept of Chem-801Sherbrooke 

Montreal, Que., H3A 2K6 

CANADA 

Telephone: 514 398-6930 

Jeremy K.M. Sanders 

Chemical Lab, Lensfield Rd 

University of Cambridge 

Cambridge, CB2 IEW 

UNITED KINGDOM 

John P. Sanders 

Physics Dept. 

San Diego State Univ. 


Telephone: 619 265-4326 

Dennis Sandoz 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Everett R Santee Jr. 

Univ of Akron 

302 E Buchtel 


Telephone: 216 375-7537 

Robert E. Santini 

Purdue University 

Department of Chemistry #92 

West Lafayette. IN 47906 

Telephone: 317 494-5230 

K.P. Sarathy 

Auburn University 


Auburn, AL 36849-5312 

Telephone: 205 826-2291 

, W 

Maziar Sardashti 

Emory University 

412 Woodruff Memorial Building 


Telephone: 404 727-5894 

Susanta K. Sarkar 


L-940, Post Office Box 1539 


Telephone: 215 270-6652 

Bruce M. Sass 


231 So. 34th St. 


Telephone: 215-898-5421 

Shiro Satoh 

Varian 

611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

John K. Saunders 

National Res Council of Canada 

Div of Biological Sciences 


CANADA 

Telephone: 613 990-0889 

Francoise Sauriol 

McGill University 

Chem Dept, 801Sherbrooke St. 

Montreal, Quebec, H3A 2K6 

CANADA 

Telephone: 514 392-5792 

Brian Sayer 

Dept of Chemistry, ANB 383 

McMaster Universlty 

Hamilton, ONT, L8P 2B4 

CANADA 

Telephone: 416 525-9140 

Jacob Schaefer 




Telephone: 314 889-6844 

Ellory Schempp 

Auburn International 

P.O. Box 2008 

Danvers, HA 01923 

Telephone: 617 777-2460 

Bob Schiksnis 


Dept of Chem 


Telephone: 215 898-4886 

Claudia Schmidt 




Telephone: 415 642-2094

Charles Schramm 

Catalytica Assoc. Inc. 

430 Ferguson Drive. Bldg 3 

Mountain View, CA 94043 

Telephone: 415 960-3000 

Suzanne E. 'Schramm 

MRDC 

P 0 Box 1025 


Telephone: 609 737-5625 

Jay F. Schulz 

Henkel Res. Corp. 

233o Circadian Way 

Santa Rosa, CA 95407 

Telephone: 717 575-7155 

Arnold L. Schwartz 


611 Nansen Way 


Telephone: 415 493-4000 

Herbert M. Schwartz 

Rensselaer Polytechnic Inst 


Troy, NY 12181 

Telephone: 518 276-6779 

Joachim Seeli~ 

Biocenter, Unlv of Basel 

Klingelbeigstr 70 

CH-4056 Basel, 

SWITZERLAND 

Mark R. Seger 

Air Products & Chemicals 

Box 538 

Allentown, PA 18195 

Telephone: 215 481-8310 

Talluri Sekhar 


Box 390, Baker Laboratory 


Telephone: 607 255-4787 

Barry S. Selinsky 

Nat. Inst. Env. Health Sci. 

MD 5-01PO Box 12233 

Research Triangle Pa, NC 27709 

Telephone: 919 541-3373 

A. J. Shaka" 



Berkeley, CA 94708-1345 

Telephone: 415-642-2094 

Xi Shan 


505 S. Mathews Ave., Box 4-I 


Telephone: 217-333-8328. 

Michael Shapiro 

Sandoz Research Institute 

NMR Facilities, Rte. 10 


Telephone: 201 503-7858 

Robert L. Sheldon 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 424-5424 

Donald R. Shepherd 

~681ifier Research 

School House Rd. 

Souderton, PA 18964-9990 

Telephone: 215 723-8181 

Barbara Sherriff 

Geology Dept., 1280 Main ST.W 


Hamilton, Ont., L8S 3M1 

CANADA 

Telephone: 6416 525-9140 

Mark Sherwood 


Dept of Chem, Henry Eyring Bld 


Telephone: 801 581-6116 

Yang Taur Shieh 


Case Western Reserve Univ. 


Ata Shirazi 



Santa Barbara, CA 93106 

Telephone: 805 961-2938 

William M. Shirley 


Wichita State Univ 

Wichita, KS 67208 

Telephone: 316 689-3120 

Ki-Joon Shon 


3601Powelton Avenue, #B-tO 


Telephone: 215 898-4886 

James N. Shoolery 


611Hansen Way 


Telephone: 415 493-4000 

Ben Shoulders 

University of Texas 


Austin, TX 78712 

Telephone: 512 471--3835 

Rajesh B Shukla 

Carnegie-Mellon Univ. 

4400 Fifth Ave./Box 87 


Telephone: 412 268-3411 

Dikoma C. Shungu 

Univ of FL School of Medicine 

Dept/Radiology, JHMHC Box J374 


Telephone: 904 392-3087 

Steve Silber 


Texas A & M University 

College Station, TX 77843 

Telephone: 409 845-1745 

Robin F. Silverman 

CIBA-GEIGY Corp. 

556 Morris Ave., Research 134 


Telephone: 201 277-5714 

James A. Simms 

MIT 

Chemistry 18-085 

Cambridge, MA 02139

Maureen Simonds 


Chem Dept 


Telephone: 413 538-2349 

Elena Simplaceanu 




Telephone: 412 268-6337 

Virgil Simplaceanu 


4400 Fifth Avenue. 


Telephone: 412 268-3396 

Larry Sims 

Univ of Houston 

4800 Calhoun. Dept of Chem 


Telephone: **** 

Dean Sindorf 

Chemagnetics 

208 Commerce Drive 

Fort Collins, CO 80524 

Telephone: 303 484-0428 

Steven W. Sinton 

Lockheed 0/9350 B/204 

3251 Hanover Street 

Palo Alto, CA 94304-1191 

Telephone: 415 424-2532 

Robert Skarjune 

3M Company 

Bldg. 201-BS-OS/3M Center 


Telephone: 612 736-9373 

Tore'Skjetne 

MR-SENTERET, SINTEF 

N-7034 Trondheim, 

NORWAY 


Cynthia M Skoglund 

John Hopkins Dniv Sch of Med 

725 N Wolfe Street 


Telephone: 301 955-3651 

Charles P S1ichter 

Univ of Illinois; Urbana-Champ 

1110 W. Green Street • 

Urbana-Champaign. IL 61801 

Telephone: 217 333-3834 

George Slomp 

The Opjohn Co 

301 Henrietta Street 


Telephone: 616 385-7431 

Steve H. Smallcombe 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Karen Ann Smith 

Colgate-Palmolive Co 

909 River Road 

Piscataway, NJ 08854 

Telephone: 201 878-7995 

Martin A.R. Smith 

Bruker Spectrospin Canada 

555 Steeles Ave. E. 

Milton, Ont., L9T IY6 

CANADA 

Telephone: 416 876-4641 

Rebecca L. Smith 

Rohm & Haas Co. Analytical Res 

727 Norristown Rd. 


Telephone: 215 641-2142 

Stanford L. Smith 

Univ of Kentucky 

Mag Res Ctr, 101 Slone Bldg 

Lexington, KY 40506-0053 

Telephone: 606 233-8993 

Steven 0 Smith 

NWI4-SIO7/MIT 

Natl Mag Lab/17O Albany St. 


Telephone: 617 253-5586 

Vane G. Smith 

ICl Americas 

Concord Pike & Murphy Road 


Telephone: 302 575-8394 

Walter Smith 

Baxter Healthcare Corp. 

6301 Lincoln Ave. 

Morton Grove, IL 60053 

Telephone: 312 965-4700 

Richard Snook 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 4}5 493-4000 

N. Soffe 

University of Oxford 

Biochemistry/South Parks Road 

Oxford, OX1 3QU 

ENGLAND 

Telephone: 44 865 275335 

Pascale Sole 




Telephone: 315 423-1021 

Mark S. Solum 

Univ of Utah 


Salt Lake City, OT 84112 

Telephone: 801 581-7351 

Sheng-Kwei Song 

Washlngton University 

Box 1134, I Brookings 

St Louis, MO 63130 

Telephone: 314 889-6583 

Christopher Sotak 




Telephone: 415 683-4393 

Steven W Sparks 


Bldg 30/Rm I06/NIDR 


Telephone: 301 496-5750 

J. B. Spitzmesser 

Dory Scientific 

600 C1emson Road 


Telephone: 803 788-6497

Richard F. Sprecher 

U.S. Dept of Energy-PETC 



Telephone: 412 892-5810 

Dr. Puliyer Srinivasan 

DuPont-NEN Products 

549 Albany St. 


Telephone: 617 350-9404 

Kathy Staudenmayer 

Eastman Kodak 

66 Eastman Avenue 


Telephone: 716 477-4132 

Edward M. Steele 

A E Staley Mfg Co 

2200 E Eldorado 

Decatur, IL 62525 

Telephone: 217 421-2141 

Paul C. Stein 

Los Alamos Nat Lab 

LANL, MS C345 

Los Alamos, NM 87545 

Telephone: 505 667-0906 

Edward O. Stejskal 

Dept. of Chemlstry, Box 8204 

North Caroline State Univ 

Raleigh, NC 27695-8204 

Telephone: 919 737-2998 

Thomas R. Stengle 

University of Massachusetts 


Amherst, MA 01003 

Telephone: 413 545-2583 

Richard Stephens 

Abbott Laboratories 

D-418, AP9 

Abbott Park, IL 60064 

Telephone: 312 937-2086 

Phoebe Stewart 



Philadelphia. PA 19104-6323 

Telephone: 215 898-3077 

Robert Stewart 

Amoco Production Co. 

4502 E 41st St PO Box 3385 

Tulsa, OK 74105 

Telephone: 918 660-4079 

Brian J. Stockman 

Univ of Wisconsin - Madison 



Telephone: 608 262-4687 

Biing-Min Su 

AKZO Chem~e America 

Livingstone Ave. 

Dobbs Ferry, NY 10522 

Telephone: 914 693-1200 

Glenn-R. Sullivan 




Telephone: 415 683-4412 

Mark J Sullivan 

Hercules Research Center 


Telephone: 302 995-3269 

Richard H. Sullivan 

Jackson State University 

PO Box 17636 

Jackson, MS 39217 

Telephone: 601 968-2171 

Susan C.J. Sumner 

NIH LC/NHLBI 



Telephone: 301 496-2350 

Boqin Sun 




Telephone: 415 642-2094 

Robert Svihla 

Wilmad Glass Co. 

Route 40 & Oak Rd. 


Telephone: 609 697-3000 

Alistair G. Swanson 

Pfizer Central Research 

Ramsgate Road 

Sandwich, Kent, CT13 9NJ 

ENGLAND 

Telephone: 0304 616672 

Scott D. Swanson 

Univ of Mich-Dept of Radiology 

Kresge Ill, R 3307 

Ann Arbor, MI 48109-0553 

Telephone: 313 936-3121 

Lydia Swenton 

G. D. Searle Co. 

4901Searle Pkwy 


Telephone: 312 982-7758 

Linda L. Szafraniec 

Chem. Res. and Dev. Center 

SMCCR-RSC-P 

Aberdeen Proving Grd, MD 21010-5423 

Telephone: 301 671-3863 

Nikolaus M. Szeverenyi 

SUNY Health Science Center 

708 Irving Avenue 


Telephone: 315 473-8470 

Lalith Talagala 

Pittsburgh NMR Institute 



Telephone: 412 647-6674 

Jau Tang 

Argonne National Laboratory 

9700 S. Lass Ave. 


Telephone: 312 972-3539 

Lim Tang-Kuan 

FDA 



Telephone: 301 496-2542 

Christian Tanzer 


Manning Park 


Telephone: 617 663-7406

Dr. June Taylor 


7701Burholme Avenue 


Telephone: 215 728-3120 

Richard B. Taylor 

Dow Corning Corporation 

Mail Stop C41D01 

Midland, MI 48686-0994 

Telephone: 517 496-5594 

Robert E. Taylor 


Manning Park 


Telephone: 617 667-9580 

~ iuke Teng 

lorida State University 

Box 251, Dept of Chemistry 


Telephone: 904 644-3254 

Takehiko Terao 


Dept of Chem 


Telephone: 415 642-2094 

Mike Tesic 


611Hansen Way 


Telephone: 415 493-4000 

V. Thanabal 

Univ of Mich-Biophy Res Div 



Telephone: 313 936-3850 

John D. Thoburn 

Univ California, San Diego 

Dept of Chem, UCSD, D-O06 

LaJolla, CA 92093 

Telephone: 619 534-3173 

William J Thoma 

University of Iowa 

Dept of Radiology 


Arthur R. Thompson 

Argonne Nat'l Laboratory 

Chemistry E169 


Telephone: 312 972-7325 

David S. Thomson 




Telephone: 203 432-3992 

Kim Thresh 

MSD Isotopes 

PO Box 899, Pte-C1aire 

Dorval; Quebec, HgR 4P7 

CANADA 

Telephone: 514 695-7920 

Hye Kyung Timken 

Mobil R&D 

Billingsport Road 

Paulsboro, NJ 08066 

Telephone: 609 423-1040 

Charles Tirendi 

4M)8 Res Inst/UCSD Med Ctr 

W. Dickinson St. 


Telephone: 619 543-6414 

Dr. S. B. Tjan 

Unilever Research Laboratorium 


3130 AC Ulaardingen, 


Telephone: 010 460-6933 

David R. Torgeson 


Ames Laboratory 


Telephone: 505 294-6353 

Daniel D Traficante 


Univ of Rhode Island 

Kingston, RI 02881 

Telephone: 401 792-5097 

Malaine Trecoske 


Dept of Chem, Latimer Hall 


Telephone: 415 642-2094 

Luc Tremblay 


2500 Boul. Universite 

Sherbrooke, Quebec, J1K 2R1 

CANADA 

Telephone: 8198217000-3099 

Rolf Tschudin 

DHHS/NIH 

Bldg. 2, I~. B2-02 


Telephone: 301 496-2692 

Candy Tsiao 

VA Polytech Inst & State Univ 

Chem Dept, VPI & SU 


Telephone: 703 961-5599 

Anne H. Turner 

Howard Univ, Dept. of Chem 

525 College St. NW 


Telephone: 202 636-6908 

Pierre Tutunjian 

Shell Dev. Co. 

P.O. Box 1380 


Telephone: 713 493-7343 

Robert Tycko 


Room 1B217, 600 Mountain Ave. 


Telephone: 201 582-7569 

Nathan R. Tzodikov 




Telephone: 415 683-4367 

Susan E Uhlendorf 

Parke Davis 

2800 Plymouth Rd 


Telephone: 313 996-7408 

Eldon L. Ulrich 




Telephone: 608 263-9498

Steve Unger 

U. C. Davis 

NMR Facility MS-1A 

Davis, CA 95616 

Telephone: 916 752-7677 

Kathleen Valentine 


Frick Chem Lab. Washington Rd. 


Telephone: 609 452-3928 

Herman Van Halbeek 

Complex Carbohydrate Ctr 

Univ. of GA/PO Box 5677 

Athens, GA 30613 

Telephone: 404 546-3312 

Craig L. VanAntwerp 

GE NMR Inst 



Telephone: 415 683-4382 

David Vander Velde 

Univ of Kansas 

Dept of Medicinal Chemistry 

Lawrence, KS 66045 

Telephone: 913 864-4187 

David VanderHart 

National Bureau of Standards 

Rm. A2Og/Bldg. 224. Div. 440 

Gaithersburg. MD 20899 

Telephone: 301 975-6754 

Peter C M Vanzijl 

Natl Inst of Health 

Bldg 10; Rm 6N105 


Telephone: 301 480-8096 

Joseph Vaughn 


1230 York Ave. 


Telephone: 212 570-7566 

David M Vea 


611Hansen Way 


Telephone: 415 493-4000 

W.S. Veeman 

Lab of Physical Chemsitry 

Univ of Nymegen, Toernooiveld 

Nymegen, 6525 ED 


Telephone: 80-613109 

Alexander J. Vega 


E356 


Telephone: 302 695-2404 

Vincent Venturella 

Anaquest/BOC Group 

100 Mountain Ave. 


Telephone: 201 771-6392 

M. Phan Viet 

Chem. Dept. PO Box 6128 Stn A 

University of Montreal 

Montreal, Que., H3C 3J7 

CANADA 

Telephone: 514 343-5857 

Fritz Vossman 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Charles G. Wade 

IBM Almaden Research K94/801 


San Jose, CA 95120-6099 

Telephone: 408 927-1650 

Gerhard Wagner 

Univ of Mich, Inst Sci & Tech 

2200 Bonisteel Blvd. 


Telephone: 313 936-3858 

John Walter 

National Research Council 

1411 Oxford St, Atlantic Res 

Halifax, N.S., B3H 3ZI 

CANADA 

Telephone: 902 426-6458 

Tom Walter 

Millipore. Waters Chrom Div 

34 Maple St 

Milford, MA 01757 

Telephone: 617 478-2000 

Dehua Wang 

Wuhan Institute of Physics 

Academic Sinica, Wuhan-Box 241 

Wuhan, Hubei, 430071 

P.R. OF CHINA 

Telephone: 812541-204 

Hsin Wang 


Bldg 82/FLI, Kodak Res. Labs 


Telephone: 716 722-4284 

Jin-shan Wanq 

Doty Scientific, Inc. 



Telephone: 803 788-6497 

Jin-shan Wang 

Virginia Tech 



Telephone: 703 961-4990 

JinFeng Wang 




Telephone: 608 262-1754 

Paul C. Wang 

Georgetown Dniv, Dept of Rdlgy 

3800 Reservoir Road, NW 


Telephone: 202 784-3415 

Shui-mei Wang 

GAF Co. 

1361Alps Rd. 

Wayne, NJ 07470 

Telephone: 201 628-3216 

Sophia Wang 




Telephone: 315 423-1021 

Yuying Wang 




Telephone: 315 423-1021

f--~ 

William W. Warren 


Room 10147 


Telephone: 201 582-2162 

Roderick E Wasylishen 

Dalhousie Univ 

Dept of Chem 

Halifax, Nova Scotia, B3H 4J3 

CANADA 

Telephone: 902 424-2564 

Andrew Waterhouse 

Tulane University 


New Orleans, LA 70118 

Telephone: 504 865-5573 

John S. Waugh 


MIT 


Telephone: 617 253-1901 

F David Wayne 

Shell Res; Thorton Res Center 

PO Box I 

Chester, CHI 3SH 

Telephone: 051 373-5665 

Andrew Webb 

Univ of Cambridge, RTC Centre 

Med Chem, Level 4 

Cambridge CB2 20Q, 

ENGLAND 

Gretchen Webb 

Yale Univ-Sterling Chem Labs 



Telephone: 203 432-3933 

ion Webb 

M-R Resources Inc 



Telephone: 617 632-7000 

Suzanne L. Wehrii 


Chem Dept-Post Office Box 413 


Telephone: 414 229-5896 

W Th Wenckebach 

Kamerlingh Onnes Lab 

PO Box 9506 

2300 RA Leiden, 

HOLLAND 


Ulrike Werner 

Univ of Calif, Berkeley 

Dept of Chem 


Telephone: 415 642-2094 

William M. Westler 




Telephone: 608 263-9599 

Roger Wheatley 

Phospho Ener~etics Inc 

2 Raymond Drlve 

Havertown, PA 19083 

Telephone: 215 789-7474 

Earl B. Whipple 

Pfizer Inc. 

Central Research Labs 

Groton, CT 06340 

Telephone: 203 441-4914 

Carol F. Wichmann 

Merck & Co. 

R80Y-345, PO Box 2000 


Telephone: 201 574-7616 

David J. Wilbur 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 424-6689 

Carl Wild 

VA Polytech Inst & State Univ 

Chem Dept, VPI & SU 


Telephone: 703 961-5599 

Joyce Wilde 

IBM 

East Fishkill Facility; Rt 52 

Nopewell Junction, NY 12533 

Telephone: 914 894-6602 

M. Robert Willcott 

NMR Imaging, Inc 

2501-C Central Pkwy, Ste. C-17 


Telephone: 713 680-8841 

Elizabeth A. Williams 

General Electric Corp R&D 

I River Rd. 

Scotia, NY 12302 

Telephone: 518 387-7856 

Evan Williams 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

Michelle Williams 

Rohm & Haas 

PO Box 219 

Bristol, PA 19007 

Telephone: 215 785-8171 

Philip G. Williams 

Lawrence Berkeley Lab 

MS 75-123, I Cyclotron Rd. 


Telephone: 415 486-7336 

Kenneth L. Williamson 


Chem Dept 


Telephone: 413 538-2349 

G. Edwin Wilson 

The Univ. of Akron 



Telephone: 216 375-7372 

Robert A. Wind 



Fort Collins, CO 80523 

Telephone: 303 491-4894 

Roland Winter 


505 S Mathews, Box 34 


Telephone: 217 333-9056

Toni Wirthlin 


611Hansen ~Y94303 

Palo Alto, 

Telephone: 415 493-4000 

William M Jr Wittbold 

Analogic Corp, Centennial Dr 

Centennial Industrial Park 


Telephone: 617 246-0300 

Donald E. Woessner 

Mobil R&D, Dallas Res Lab 

13777 Midway Road 

Dallas, TX 75244 

Telephone: 214 851-8166 

Roger A. Wolfe 

Occidental Chemical Corp 

2801 Long Road 

Grand Island. NY 14072 

Telephone: 716 773-8551 

Gerd Wolff 

Bruker Medical Instruments 

Mannin 9 Park 


Telephone: 617 667-9580 

Alan Wolfson 


Mannin~ Park 


Telephone: 617-667-9580 

Kurt Wollenberg 

Lubrizol Corporation 

29400 Lakeland Boulevard 

Wickliffe, OH 44092 

Telephone: 2169434200X2026 

Sam T. S. Wong 

U of Cal-Lawrence Berkeley Lab 

MS 55-121, Cyclotron Road 

Berkeley, C~ 94720 

Telephone: 415 486-6114 

Kyu Whan Woo 



Telephone: 217 244-4248 

Bruce Woods 

PQ Corporation 

280 Cedar Grove Road 

Lafayette Hill. PA 19444 

Telephone: 215 941-2071 

Gang Wu 

York University 

Dept of Chem. 4700 Keele St. 

North York, Ontario, M3J IP3 

CANADA 

Telephone: 416 736-2100 

Ping Pin Yang 

PITMAN-MOORE, Inc.-IMC 

PO Box 207 

Terre Haute, IN 47808 

Telephone: 812 230-0121 

Constantino Yannoni 




Telephone: 408 927-2450 

Dr. Phillip Yeagle 

State U of NY at Buffalo 

Biochem Dept 102 Cary Hall 

Buffalo, NY 14214 

Telephone: 716 831-2700 

James Yesinowski 

Calif Inst of Tech 

MC 164-30 

Pasadena, CA 91125 

Telephone: 818 356-6241 

Hong N. Yeung 

Univ of Mich Nosp-Dpt of Radlg 

Kresge III, R3307 

Ann Arbor, MI 48109-0553 

Telephone: 313 747-0846 

Gregory Young 

Wright State University 

3525 Southern Boulevard 

Kettering, OH 45429 

Telephone: 513 299-7204 

Gregory Yvars 


Millis Science Ctr 


Telephone: 216 368-5917 

Michael G Zagorski 

Biochem. Dept, 630 W 168th St. 

Columbia University 


Telephone: 212 305-5280 

Michael Zehfus 


420 Henry Mall 


Telephone: 608 263-9498 

Andrew S. Zektzer 

Abbott Laboratories 

D-418 

Abbott Park, IL 60064 

Telephone: 312 937-2083 

Toby Zens 


611Hansen Way 


Telephone: 415 493-4000 

Melodee Zentner 

Morton Thiokil, Inc. 

1275 Lake Ave. 

Woodstock, IL 60098 

Telephone: 815 338-1800 

Kurt W. Zilm 


Dept of Chem-225 Prospect St. 


Telephone: 203-432-3956 

Nicholas Zumbulyadis 


Corp Res Labs, Bldg 82 Rm C204 


Telephone: 716 722-1409 

Maruta Zvagulis 

University of Auckland 

Auckland, 

NEW ZEALAND 

Telephone: 217 333-2535

th  - 1988 - 51st ENC Conference

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?