th  - 1987 - 51st ENC Conference

28 th �� - 1987 Asilomar 

Chair: Lynn Jelinski 

Local Arrangements: Lynne Batchelder 

A summary of the 28 th ENC, presented as a “virtual interview:” 

Ted Becker: The 28 th in 1987 had some curious aspects. For 

example, why did the technical program begin on Sunday night? In 

all the previous years it had started on Monday morning. 

Lynn Jelinski: I was afraid you’d ask about that. The early start 

was to fix a faux pas on my part. Somehow we neglected to invite 

Richard Ernst to speak until all of the slots were full. 

Ted: Having him speak was a good idea; Richard went on to win 

the Nobel Prize in Chemistry in 1991 for his pioneering work in high 

resolution NMR. 

Lynn: It turns out that three future Nobel Prize winners attended the 28 th ENC. Kurt Wüthrich 

would go on to win the Nobel Prize in Chemistry in 2002 for his contributions for the determination 

of the 3D structure of biological macromolecules in solution, and Paul Lauterbur in Physiology or 

Medicine for his pioneering work on MRI. Active participation by all three future Nobel Prize 

winners underscores the high profile and value of the ENC as a vehicle for communicating new 

developments in NMR. 

Ted: What were some of the firsts of the 28 th ENC? Things that an attendee might not have 

noticed? 

Lynn: It was the first year that the ENC employed a professional conference organizer, with 

somewhat mixed results. That was before Judith, of course. We also introduced the Monterey 

cypress logo, which I clipped from a California tourism magazine and Xeroxed onto the cover of 

the program. (Ed Stejskal hand-lettered the cover in his famous calligraphy.) I’ve been worried 

ever since 1987 that someone would nab me for copyright infringement. I’m delighted to see that 

the ENC’s logo today still retains the spirit of our first logo. 

28 th 

ENC 

Ted: The symbolism is powerful as we celebrate the 50 th ENC. As I recall, you wrote: “The 

Monterey cypress, an evergreen that thrives on the Monterey Peninsula, …, symbolizes a special

location where people in a never-dormant field return year after year to discuss the newest 

developments in NMR.” 

Lynn: You can tell that I was heavily influenced by the Jiri Jonas, Herb Gutowsky monograph, 

NMR, an Evergreen. 

Ted: There must be some other interesting behind-the-scenes vignettes you’d like to share about 

the 28 th ENC. 

Lynn: Let’s see – there were a couple of exciting things. The fire alarm went off during one of 

the talks. Even though we guessed that it was a false alarm, we couldn’t take a chance and 

evacuated anyway. Then there was the quip I overhead the first night after what turned out to be an 

unintentional (on my part) parade of women leading off the ENC. It began with me welcoming 

everyone to the 28 th ENC, Lynne Batchelder serving as the all-important local arrangements 

coordinator, Linda Sweeting chairing the first technical session, and Mary Baum running the brief 

oral summaries of the posters. I overheard someone say, “Oh, my goodness. What happened to the 

men?” 

Ted: Those were changing times. What about the historical context of the conference? 

Lynn: It’s hard to believe that 1987 was before widespread use of e-mail, and that PowerPoint 

1.0 was introduced in April of that year. But some things were prophetic for our current times. For 

example, one of the sessions dealt with “NMR for the Detection of Explosives,” and 1987 would be 

the year of Black Monday, when the Dow Jones Industrial Average dropped 22.6% of its value in 

one day. 

Ted: Do you have any parting comments as we celebrate the 50 th ENC? 

Lynn: I am heartened to see that the ENC continues to attract really talented people driven to 

make new contributions to NMR. I can recall my first ENC (the 19th, in Blacksburg, in 1978) 

where one of the talks was entitled “2D or not 2D?” Hard to imagine, isn’t it? The preponderance 

of new people at the 50 th ENC and the strong history of past programs underlie that fact that NMR 

truly is an evergreen.

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Contributors to the 28th ENC 

The Organizing Committee is extremely grateful to the following vendors for 

their financial support of this ENC. 

Academic Press 

Aldrich Chemical Company 

Amplifier Research 

Bruker Instruments, Inc. 

Cambridge Isotopes, Inc. 

Doty Scientific, Inc. 

Eastern Analytical Symposium 

Electronic Navigation Industries, Inc. (ENI) 

General Electric Company, Medical Systems Group 

ICN Biochemicals 

ICON Services, Inc. 

JEOL (USA) Inc. 

John Wiley and Sons 

Marcel Decker Press 

Merck Sharpe and Dohme, Isotopes 

M-R Resources 

New ERA Enterprises 

New Methods Research 

N'MR Concepts 

NOVEX, Inc. 

Oxford Instruments North America, Inc. 

Pergammon Press 

Phospho-Energetics, Inc. 

Programmed Test Sources (PTS) 

Scientific Information Services 

Sciteq Electronics, Inc. 

Siemens Medical Systems 

Spectral Data Services 

Strawberry Fields 

Tecmag, Inc. 

Trident Computer Corporation 

Varian Associates 

Wilmad Glass Company 

cover deaign by Ed Stejskai: The Monterey 

cypress, an evergreen that thrives on the 

Monterey Peninsula, against the color of the 

Pacific Ocean, symbolizes a special location 

where people in a never-dormant field return 

year after year to discuss the newest 

developments in N-IVIR.

Program for the 28th ENC 

April 5-0, 1987 

Asilomar, California 

Chair: Lynn IV. Jelinski 

Local Arrwzgements Chair: Lynne S. Batchelder 

• Regular sessions will take place in Merrill Hall, with simultaneous video transmission to 

the Chapel for overflow. 

• Posters should be set-up on Sunday afternoon in Firelight Forum and Kiln, and will remain 

up for the entire conference. There will be two poster sessions, one on Monday afternoon, 

and the other on Wednesday afternoon. 

• Breakfast will be served continuously from 7:00 -9:00 am. There will be two seatings for 

Lunch (12:00 n and 1:00 pm) and two seatings for Dinner (5:30 pm and 6:30 pm). The 

Banquet will be held on Wednesday evening at 7:00. Tickets may be purchased for $15. 

Sunday Afternoon 

3:00-6:00 

Sunday Evening 

7:30 

7:40 

8:30-0:30 

Lyre1 IV. Jelinski 

Linda Sweeting, Chair 

R. R. Ernst 

A. Schweiger 

R. Briischweiler 

C. Biihlmann 

J.-M. Fauth 

C. Gemperle 

C. Griesinger 

R. Kreis 

Z. Mddi 

J. C. Madsen 

B. U. Meier 

S. Pfenninger 

C. Radloff 

C. Sch6nenberger 

O. W. Sorensen 

W. Studer 

A. Thomas 

Mary Baurn, Chair 

Jewl Baum 

C. M. Dobson 

C. Hanley 

P. A. Evans 

Registration; registration mixer in Viewpoint 

Welcoming Remarks 

Opening Session 

Time Domain Magnetic Resonance. An Appreciation 

of Current Trends in NMR and ESR 

POSTERS (Preview Of STellar PostERS) 

NMR Studies of a-Lactalbumin: Characterization of a 

Partially Unfolded State. Poster MKI

Monday Morning 

8:30 - 10:00 

10:00 - 10:30 

10:30 - 12:00 

Monday Afternoon 

James E. Roberts 

T. G. Neiss 

Ronald M. Jarret 

M. Saunders 

Oded Gonen 

P. Kuhns 

P. C. Hammel 

J. S. Waugh 

Karen K. Gleason 

M. A. Petrich 

J. A. Reimer 

Start Opella, Chair 

K. Wfithrich 

C. M. Dobson 

A. M. Gronenborn 

G. M. Clore 

-- break -- 

Mike Maddox, Chair 

Thomas L. James 

Brandan Borgias 

Ei-ichiro Suzuki 

Ning Zhou 

Anna Maria Biannuci 

Gerald Zon 

Neils Anderson 

Hugh L. Eaton 

Khe Nguyen 

Philip H. Bolton 

2:00 - 5:00 Mary Baum, Chair 

--wine and cheese-- 

Increased Resolution for Proton NMR Spectra of Solid 

Materials. Poster MF33 

Di-xaC Labeling: A Means to Measure 12C-~aC Isotopic 

Equilibria in the 2- Norbornyl Cation. Poster MF53 

NMR Spectroscopy Below I K. Poster MF3 

NMR Investigations of Atomic Microstructure in 

Amorphous Semiconductors. Poster MF23 

Protein NMR 

Determination of Protein Structures in Solution by 

NMR 

Protein Dynamics and Folding Studied by 

Magnetization Transfer NMR 

Determination of Three-Dimensional Structures of 

Proteins in Solution 

Determination of Molecular Conformation in Solution 

by 2-Dimensional NMR Spectroscopy. 

Structure and Dynamics Using Complete Relaxation 

Matrix Analysis of 2D NOE Spectra. 

Conformations of Molecules in the Protein--Bound 

State 

NOE Studies 

Presenters of Poster Session M will be available for 

discussion in Firelight Forum and Kiln

Monday Evening 

7:30 - 9:00 A. N. Garroway, Chair 

Tuesday Morning 

8:30 - 10:00 

10:00 - 10:30 

10:30 - 12:00 

Ann T. Nicol 

Robert M. Pearson 

Lyn Ream 

Constantin Job 

IV. L. Rollwitz 

Armando De Los Santos 

George A. Matzkanin 

J. Derwin King 

Andy Byrd, Chair 

Jeffrey C. Hoch 

Ernest D. Laue 

G. Bodenhausen 

Peter Pfiindler 

Marjana Novic 

Hartmut Oschkinat 

Steve Wimperis 

Guy Jaccard 

Urs Eggenberger 

Dominique Limat 

-- break -- 

Ad Bax, Chair 

David Cowburn 

William M. Westler 

John L. Markley 

NMR in Mobile Systems: Mobile Samples and Mobile 

Spectrometers 

The NIVIR Gyro: Application of NMR in a Slowly 

Rotating Frame 

Industrial Magnetic Resonance (IMR): A Magnetic 

Resonance Spectrometer Built as an Industrial Process 

Controller 

NMR for the Detection of Explosives 

Current Applications of Computing in NMR 

Spectroscopy: Utilization of Mini- and Main-Frames 

for Data Analysis by Conventional and Non- 

conventional Approaches 

Why Is Software So Hard? A Contrary View of NMR 

Data Processing 

Selective Data Sampling: Application to 2D NMR 

Pattern Recognition in High-Resolution 2D NMR 

Spectra: A Closer Look at Cross-Peaks 

How to Sense Your Low Gammas 

Indirect Detection of lSN and x3C: Instrumental 

Considerations and Biochemical Applications 

Proton-Detected Heteronuclear One-and Two- 

Dimensional NMR Spectra of Biomolecules: Shift 

Correlation and Relaxation Measurements

C. Griesinger Novel Approaches to Three-Dimensional NIVlR 

Tuesday Afternoon -- free time -- 

Tuesday Evening 

7:30 - 8:30 

8:30 - 9:30 

Wednesday Morning 

N. Zumbulyadis, Chair 

J. S. Waugh 

C-G. Tang 

Robert A. Wind 

Steven F. Dec 

Gary E. Maciel 

D. Suter 

Mary Baum, Chair 

Bernhard Bliimich 

C. Schmidt 

S. Kaufmann 

S. Wefing 

D. Theimer 

H. W. Spiess 

Ole W. Sorensen 

C. Griesinger 

C. Gemperle 

R. R. Ernst 

Peter A. Mirau 

Malcolm Levitt 

M. F. Roberts 

Charles L. Dumoulin 

S. P. Souza 

H. R. Hart, Jr. 

Gauss Meets Angstrom: Spatial and Spectral Spin 

Diffusion 

Spatial and Spectral Diffusion of Magnetization 

Suppression of Dipolar Broadening by Magic Angle 

Spinning 

Diffusion of Spin Order in Resolved Solid State NMR 

Spectra 

POSTERS 

2D Exchange NMR in Non-Spinning Powders. Poster 

WF54 

Symmetry and Antisymmetry in 2D NMR Spectra. 

Poster WKI4 

Quantitative Interpretation of a Single 2D NOE 

Spectrum. PosterWK12 

Solvent Suppression Without Phase Distortion. Poster 

WK22 

NMR Flow Imaging. Poster WF64 

8:30 - 10:00 Ed Stejskal, Chair CPMAS, And Then Some

10:00 - 10:30 

10:30 - 12:00 

C. S. Yannoni 

H. Seidel 

R. D. Kendrick 

M. E. Galvin 

J. P. Yes#~owski 

H. Eckert 

A. Nayeem 

G. S. Harbison 

V.-D. Vogt 

C. Boeffel 

B. Bluemich 

H. W. Spiess 

R. G. Griffin 

A. C. Kolbert 

D. P. Raleigh 

M. H. Levitt 

-- break -- 

L. S. Batchelder, Chair 

J. L. Ragle 

Ann M. Thayer 

Paul D. Ellis 

Paul D. Majors 

Thomas E. Raidy 

Paul S. Marchetti 

Alan Benesi 

Doug Morris 

Shelton Bank 

Richard Adams 

IF. S. Veemmz 

R. Janssen 

E. Tijink 

A. P. M. Kentgens 

Surface-Selective NMR by Dynamic Nuclear 

Polarization. Exploration at the Polymer Interface. 

High-speed 1H MAS--NMR of Inorganic Solids and 

Paramagnetic Compounds 

The Determination of the Structure of Partially- 

Oriented Solids Using 2D--Magic-Angle-Spinning 

NMR. 

Multiple Pulse Echo Trains in Rotating Solids 

Quadrupolar Interactions in the Solid State. 

Field Cycling NMR at a Tool for NQR Spectroscopy 

of Weakly Quadrupole-Couoled Nuclei: Pyridine, 

Imidazole, and the Nucleosides Adenosine, Guanosine 

and Inosine. 

Applications of Zero Field NMR to the Study of Solids 

and Liquid Crystals 

Applications of Solid State NMR Methods to Problems 

of Interest to Surface Chemistry 

Quadrupole Nutation NMR, NQR in the Rotating 

Frame

Wednesday Afternoon 

2:00 - 5:00 Mary Baum, Chair 

Wednesday Evening 

-- refreshments -- 

6:00 Cocktail Hour 

7:00 Banquet 

Thursday Morning 

H. S. Gutowsky 

8:30 - 10:00 Robert Bryant, Chair 

D. I. Hoult 

G. Glover 

Peter R. Luyten 

Jan A. den Hollander 

10:00 - 10:30 --break -- 

10:30 - 12:00 N. Szeverenyi, Chair 

Warren S. Warren 

D. P. Weitekamp 

David Andrew 

Presenters of Poster Session W will be available for 

discussion in Firelight Forum and Kiln 

Merrill Hall 

"... no sign of slackening" 

Spatially Resolved Spectroscopy 

An Overview of Spatially Resolved Spectroscopy 

Transient Gradient Effects 

Image Guided Localized NMR Spectroscopy at 1.5 T. 

Gizmos 

Pulse Shaping for Two-Dimensional and Multiple Pulse 

Spectroscopy 

Coherence Augmentation by Limiting the Entropy in 

Catalytic Hydrogenation 

Active Shield Magnets for Magnetic Resonance 

Imaging

Sunday - PM 

TIME DOMAIN MAGNETIC RESONANCE 

AN APPRECIATION OF CURRENT TRENDS IN NMR AND ESR 

R.R. Ernst, A. Schweiger, R. BrUschweiler, 

C. BUhlmann, J.-M. Fauth, C. Gemperle, 

C. Griesinger, R. Kreis, Z. M~di, J.C. Madsen, 

B.U. Meier, S. Pfenninger, C. Radloff, 

C. Sch~nenberger, O.W. S~rensen, W, Stude~, A. Thomas 

Laboratorium fur Physikalische Chemie 

Eidgen~ssische Technische Hochschule 

8092 ZUrich, Switzerland 

A few introductory remarks are made in order to high- 

light the importance of time domain experiments in magnetic 

resonance. A comparison of features of NMR and ESR relevant 

in this context is given. In particular the challenges, op- 

portunities and limitations of pulse ESR are discussed in 

view of the nowadays well established pulse technology of 

NMR. 

A potpourrie of techniques recently developed at ETH is 

presented including ESR techniques such as electron spin echo 

spectroscopy with jumping field vectors, Mz-detection, hyper- 

fine-selective pulse ENDOR, and NMR techniques such as com- 

puter pattern recognition, 2D rotating frame experiments, 

selective 2D spectroscopy and rf pulse-excited zero field 

magnetic resonance.

Sunday - PM 

MKI - POSTERS 

STUDIES OF Q-LAC'I"ALB~IIN: 

(~A~ZATTON OF A PARTIALLY I~rP~LD~ STATE 

J. Baum; C.M. Dobson, C. Hanley 

Inorganic Chemistry Laboratory 

University of Oxford 

Oxford, ENGLAND 

P.A. Evans 

Middlesex Hospital Medical School 

London, ENGLAND 

To understand the folding mechanism of proteins, it is 

important to characterize, at the molecular level, the 

structures of states "intermediate between the folded and 

unfolded conformations. Incompletl¥ folded proteins tend to 

have very small IS chemical shift dispersions, therefore 

methods have been developed to probe these intermediate states 

indirectly via the well-resolved IH spectrum of the native 

protein. Guinea-pig G-lactalbumin provides an especially 

favourable system for the investigation of folding due to its 

sensitivity to solution conditions; within certain ranges of pH 

and temperature there exists a stable partially unfolded 

intermediate which we can study by NMR. PH-jump hydrogen 

exchange experiments are being developed to assign indirectly, 

through the native protein, the labile protons of the unfolded 

state, and magnetization transfer experiments are used to 

correlate the resonances of the unfolded protein with those of 

the native protein. These and other experiments have allowed 

us to identify regions of localized structure at the individual 

residue level in the unfolded form of G-lactalbumin.

Sunday - PM 

MF33 - POSTERS 

INCREASED RESOLUTION FOR PROTON NMR SPECTRA OF SOLID MATERIALS 

Thomas G. Neiss and James E. Roberts 

Department of Chemistry #6 

Lehigh University 

Bethlehem, PA 18015 

Sophisticated multiple-pulse techniques must be used to 

obtain "high resolution" proton spectra of most solid 

materials, or a single broad peak is observed as a consequence 

of the large homonuclear couplings of the proton reservoir. 

When Magic Angle Sample Spinning (MASS) is included with the 

multiple-pulse experiment, the typical proton peak width is 

still between 1 and 2 ppm. When several isotropic chemical 

shifts are present, the resulting spectrum is often not 

interpretable due to significant spectral overlap. Two more 

complicated experiments are available for increasing the 

resolution obtained in proton NMR spectra of solid materials. 

Two-dimensional heteronuclear chemical shift correlation 

NMR has been applied to liquids to connect the proton and 

carbon chemical shifts through J couplings. The J couplings 

in solids are usually not resolved. However, with appropriate 

implementation during MASS, the 2-D experiment correlates the 

proton and carbon chemical shifts, yielding better overall 

resolution in the proton dimension, even though the proton 

linewidths are still 1 to 2 ppm. 

An alternative to the full two dimensional technique 

utilizes selective coherence transfer to observe only specific 

spin systems in a one-dimensional experiment. The selective 

coherence transfer occurs through the strong heteronuclear 

dipolar interaction between bonded spins, so some protons are 

not readily observed with this technique. The gain in proton 

spectrum resolution is comparable to that obtained with 

two-dimensional chemical shift correlation, but data 

accumulation and processing takes less time. Although several 

I-D selective experiments might be needed to fully 

characterize a molecule, it is still a viable approach in many 

situations. 

Acknowledgement is made to the donors of the Petroleum 

Research Fund for partial support of this work. Supported by 

NSF-Solid State Chemistry program grant # DMR-8553275. 

Additional support through the Presidential Young Investigator 

program was obtained from Cambridge Isotope Laboratories; Doty 

Scientific; General Electric Corporate Research and 

Development; General Electric NMR Instruments; IBM 

Instruments; Merck, Sharp and Dohme; and Monsanto Company.

Sunday - PM 


DI-13C-LABELING: A MEANS TO MEASURE 12C-13C 

ISOTOPIC EQUILIBRIA IN 2-NORBORNYL CATION. 

Ronald M. Jarret*, Department of Chemistry, College of the 

Holy Cross, Worcester, MA 01610. 

Martin Saunders, Department of Chemistry, Yale University 

New Haven, CT 06511. 

2,3-Di-13C-norborn-2-yl chloride was prepared and ' 

ionized (with SbF~) to 2-norbornyl cation. In solution 

at -65°C, rap~ r~arrangements occur which completely 

scramble the C-labels. The proton-decoupled cmr 

rspectrum (62.7 MHz) contains three signals: C-4, C-I,2,6 

(averaged), and C-3,5,7 (averaged). The 13C-labels are 

thus equilibrated over nonrequivalent sites within 

2-norbornyl cation. This IZC-13C equilibrium isotope 

effect alters the proportion of di-13C-labeled isomers 

from statistical values. The non-statistical isotopic 

isomer population is manifested as an asymmetric 

multiplet for the averaged C-3,5,7 peak in the cmr 

spectrum. The relatively sharp lines of the multiplet 

can be reproduced within ± 0 . 1 ppm, with isotopic 

equilibrium constants of K-3,5,7 = 1.010 ± 0.005 and 

K-I,2,6 = 1.039 ± 0.005. 

7 4 

5 3 

6 CI(H) 

H(CI)

Sunday - PM 

MF3 - POSTERS 

NMR SPECTROSCOPY BELOW 1K 

Oded Gonen*, P. Kuhns, P. C. Hammel and J. S. Waugh 

Department of Chemistry 

Massachusetts Institute of Technology 

Cambridge, Massachusetts 02139 

L. Boltzmann tells us that large (>104 ) gains in NMR sensitivity can be 

obl;ained by lowering the temperature to -yhBo/k, a few millikelvin. We will 

present a selection of results obtained in pursuit of this goal, to illustrate 

the following points: 

>T1, previously expected to be astronomically large, is quite acceptably 

short in powdered samples immersed in liquid 3He. 

>Signals are indeed large: sometimes nearly a volt directly from the 

probe. Monolayers of adsorbed species give strong spectra in a single shot. 

mometer. 

>The shape of the spectrum provides a convenient self-calibrating ther- 

>The usual FT relation between the FID and the spectrum is modified at 

low temperatures. 

>Spin-spin relaxation is sometimes anomalously slow.

Sunday - PM 


NMR INVESTIGATIONS OF ATOMIC MICROSTRUCTURE 

IN AMORPHOUS SEMICONDUCTORS 

Q 

Karen K. Gleason , Mark A. Petrich, and Jeffrey A. Reimer, 

Department of Chemical Engineering, University of California, 

Berkeley, CA 94720-9989. 

The microstructure of amorphous semiconductors has important 

implications for their electronic properties. Nuclear magnetic 

resonance (NMR) can examine the microstructure of these materials 

on an atomic scale. Previous NMR results have indicated that the 

hydrogen in these materials exists both as isolated hydrogen atoms 

and as clusters of hydrogen. Using Multiple Quantum NMR, a 

technique which is able to "count" the number of hydrogen atoms in a 

cluster, we have studied the effects of deposition temperature, 

dopant atoms, and annealing on the clustering of hydrogen in 

amorphous silicon. Our results indicate that electronic device 

quality amorphous silicon films contain small clusters of 

approximately six hydrogen atoms, while nondevice quality films 

contain larger hydrogen atom clusters. We have also extended the 

multiple quantum NMR technique to study a series of amorphous 

silicon carbide alloys, systematically varied in carbon content. We 

have found that small amounts of carbon decrease the total hydrogen 

content of the alloy, but increase hydrogen clustering. Carbon-13 

and silicon-29 magic-angle spinning NMR spectra, taken with and 

without proton decoupling, allow us to probe local bonding 

configurations. These studies have shown that both sp 2 and sp 3 

carbon bonding environments are important in these materials. It is 

especially interesting that nearly all the hydrogenated carbon are 

in the sp 3 bonding configuration. 

By comparing our NMR results with data from other analytical 

techniques such as infrared and optical absorption spectroscopy, 

Rutherford backscattering, and conductivity measurements, we hope 

to elucidate the relationships between deposition chemistry, atomic 

microstructure, and optoelectronic properties of this 

technologically important class of materials. 

Supported by NSF grant DMR-8304163. 

8

Monday - AM 

Determination of Protein Structures in Solution by NMR 

K. Wathrich 

Institut fClr Molecularbiologie und Biophysik 

E.T.H.-H~nggerberg 

CH-8093 Z~'ich, Switzerland 

During the period 1979-83 methods were introduced for efficient sequence-specific 

assignment of the 1H NMR spectra of proteins and nucleic acids in solution. This now provides 

the basis for determination of the three dimensional structure of these biological macromolecules 

(K. Wgthrich, NMR of Proteins and Nucleic Acids, Wiley, New York, 1986). This method for 

structure determination will be surveyed, and novel approaches making use of isotope labeling and 

X-filtering techniques will be described.

Monday - AM 

Protein Dynamics and Foldlng Studied by Magnetization Transfer NMR 

Christopher M. Dobson 



South Parks Road 

Oxford OXI 3QR 

England 

NMR provides an experimental basis for investigating in 

considerable detall the structures and dynamics of biological molecules 

in solutlon. As part of our studies of the folding and unfolding of 

globular proteins, we have been explolting magnetization transfer 

processes in both one- and two-dlmenslonal NMR experiments. 

The procedures have been establlshed in studies of lysozyme, where 

accurate rate constants for both 

determined by following the time 

saturation transfer experlments I. 

effects in two-dlmensional NOESY 

folding and unfolding have been 

developments of one-dlmenslonal 

In addition, chemical exchange 

experiments have permitted the 

correlation of resonances in folded and unfolded states, permitting 

assignment and interpretation of the spectrum of the unfolded state 

through the extensive knowledge of the spectrum of the folded state 2. 

These techniques have been applied to the study of a number of 

other proteins. In the case of one of these, staphylococcal nuclease, 

two distinct conformations of the folded form exist in equillbrium. 

One- and two-dimenslonal magnetization transfer experiments have 

demonstrated the interconversion of these two states with each other and 

with two unfolded states 3. Further, one dlmenslonal multlple saturation 

techniques have been used to explore the kinetics of the interconverslon 

of the different states, and to explore the re]atlve significance of 

different pathways of folding and unfolding. A structural basis for the 

observed behaviour has been proposed and is supported by the results of

slte-dlrected mutagenesls experlments 4. The experiments have therefore 

permitted specific dynamical events in the foldlng of a protein to be 

defined. 

I. 

2. 

3. 

4. 

C.M. Dobson and P.A. Evans, Biochemistry 2_~3, 4267 (1984) 

C.M. Dobson, P.A. Evans and K.L. Willlamson, FEBS Letters 168, 331 

(1984); C.M. Dobson, P.A. Evans, C. Redfleld and K.D. Topping, to 

be published. 

R.O. Fox, P.A. Evans and C.M. Dobson, Nature 320, 192 (1986) 

C.M. Dobson, P.A. Evans and R.0. Fox, to be publlshed.

Monday - AM 

Abstract" 28th ENC, Asilomar, April 5-9, 1987 

DETERMINATION OF THREE-DIMENSIONAL STRUCTURES OF PROTEINS IN 

SOLUTION 

A.M. Gronenborn and G.M. Clore 

Max-Planck Institut fur Biochemie, ~8033 Martinsried bei Munchen, 

F.R.G. 

The determination of 3D-structures of proteins in solution using 

NMR spectroscopy comprises three stages: (i) the assignment of 

proton resonances by 2D-techniques to demonstrate through-bond and 

through-space connectivities; (ii) the determination of a large 

number of short (< 5A) interproton distances using nuclear 

Overhauser effect (NOE) measurements; and (iii) the determination 

of the 3D-structure on the basis of these distances. Our approach 

for step (iii) has involved the use of restrained molecular 

dynamics. The principles of the restrained dynamics approach will 

be illustrated for model calculations on crambin (1,2) and examples 

from the set of 3D-structures in solution that we have determined 

to date will be presented: purothionin (3), phoratoxin (4), hirudin 

(5), the globular domain of histone H5 (6), growth hormone 

releasing factor (7), secretin and potato carboxypeptidase 

inhibitor. 

References: 

I. Brunger, A.T., Clore, G.M., Gronenborn, A.M. & Karplus, M. 

(1986) Proc° Natl. Acad. Sci. U.S.A. 83, 3801-3805 

2 Clore, G.M. Brunger, A.T., Karplus, M. & Gronenborn, A.M. (1986) 

J. Mol. Biol. 191, 523-551 

3 Clore, G.M., Nilges, M., Sukumaran, D.K., Brunger, A.T., 

Karplus, M. & Gronenborn, A.M. (1986) EMBO J. 5, 2729-2735 

4 Clore, G.M., Sukumaran, D.K., Nilges, M. & Gronenborn, A.M. 

(1987) Biochemistry in press 

5 Clore, G.M., Nilges, M., Sukumaran, D.K., Zarbock, J & 

Gronenborn, A.M. (1987) EMBO J. in press 

6 Zarbock, J, Clore, G.M. & Gronenborn, A.M. (1986) Proc. Natl. 

Acad. Sci. U.S.A. 83, 7628-7632 

7 Clore, G.M., Martin, S.R. & Gronenborn, A.M. (1986) 

J. Mol. Biol. 191, 553-561

Monday - AM 

STRUCTURE AND DYNAMICS USING COMPLETE RELAXATION MATRIX 

ANALYSIS OF 2D NOE SPECTRA 

Thomas L. James, Brandan Borgias, Ei-ichiro Suzuki, Ning Zhou, Anna Mafia Biannuci and 

Gerald Zon, Departments of Pharmaceutical Chemistry and Radiology, University of California, 

San Francisco, CA 94143 

Of all possible techniques, 2D NMR has the greatest capability for structural charac- 

terization of moderate size molecules (_

Monday - AM 

CONFORMATIONS OF MOLECULES IN THE PROTEIN-BOUND STATE 

Niels H. Andersen*, Hugh L. Eaton and Khe Nguyen 

Department of Chemistry, University of Washington, Seattle, WA 98195 

The pure absorption phase 2D spin-exchange experiment (PS-NOESY) is 

ideally suited for measuring exchange-transferred NOEs (which reflect the 

bound-state geometry) for small molecules in rapid exchange with a 

protein-ligand complex. The 2D data matrix holds within it all possible 

control spectra and frequency-tailored streak correction methods (using 

sums and differences of columns and rows) can remove spin-diffusion 

"artifacts" associated with the perturbation of frequency coincident 

protein resonances. We will show how bound-state cross-relaxation rates 

can be derived from 2D experiments that require less than three hours of 

data accumulation at 6-10mM_ ligand concentrations. The techniques will 

be illustrated with NAD/oxidoreductrase complexes and with tryptophan and 

prostaglandin Fp~ bound at their specific receptors sites on serum 

albumin. In the case of L-tryptophan, a single bound-state conformation 

(which does not correspond to the major conformer in free aqueous 

solution) has been determined. The conformation elucidation utilized 

NOE data at the complete r_elaxation_matrix a__nalysis (CORMA) level rather 

than making the linear limit "isolated spin pair" assumption. 

Data reduction strategies suitable for 2D NOESY experiments acquired 

with severely truncated preparatory delays will be presented. The 

methods include multispin effects and provide an alternative to CORMA for 

initial estimated of relaxation and cross-relaxation rates. Computer 

simulations that reveal the "errors" associated with the "isolated spin 

pair" and "two step cross-relaxation" approximations will be presented.

Monday - AM 

NOE STUDIES 

Philip H. Bolton 


Wesleyan University 

Middletown, CT 06457 

This talk will contain overviews of our progress in three projects which 

involve either the use of NOEs to determine conformational features of 

proteins, the development of novel NOE experiments or the analysis of the 

data from NOE experiments. 

Staphylococcal nuclease and proteins formed by single site amino acid re- 

placement of residues at the active site have been investigated by two- 

dimensional NOE spectroscopy. The use of residue specific labeling has been 

crucial to progress in this area as it is the only means available for 

unambiguous assignment of the NOE cross-peaks of the proteins which contain 

149 amino acids. 

Low field NMR is a procedure by which the NOEs are generated in a very low 

field, typically 60 MHz, whereas the equilibration and detection are at 400 

MHz. When the NOE transfer occurs in such a low field there are no compli- 

cations due to multiple correlation times or spin diffusion and the NOEs 

from macromolecules are as simple to interpret as the high field NOEs of 

small molecules. 

Image analysis of two-dimensional data sets can exploit both the global and 

local symmetry of the signals to arrive at enhanced signal-to-noise as well 

as to determine which spin systems are present.

Notes

Monday - PM 

The NMR Gyro: An Application of NMR in a 

Slowly Rotating Frame 

Ann T. Nicol 

Litton Guidance and Control Systems 

5500 Canoga Avenue 

Woodland Hills, CA 91367 

The NMR gyro is a device which senses rotations through 

changes in frequency (or phase) of an NMR signal as a result of 

rotations relative to the inertial precession of a nuclear 

magnetic moment. Mechanization of such a device requires that 

the entire NMR ',spectrometer" undergoes the rotation and that 

this "spectrometer" be compact, occupying only a few cubic 

inches. This condition is realized in systems where a fairly 

high degree of nuclear polarization is achieved in very low 

fields (less than I gauss). The approach uses isotopes of noble 

gases and the nuclear polarization is achieved through a cross 

polarization with optically pumped alkalis. This presentation 

will discuss the basic physical principles of the NMR gyro and 

will present experimental results on the processes and 

interactions governing nuclear polarization and relaxation in 

such systems. 

References 

I. A.T. Nicol, Phys. Rev. B 29, 2397 (1984). 

2. T.M. Kwon, J.G. Mark, and C.H. Volk, Phys. Rev A 24, 1894 

(1981).

Monday - PM 

Industrial Magnetic Resonance (IMR) 

A Magnetic Resonance Spectrometer built as an 

Industrial Process Controller 

Robert M. Pearson, Lyn Ream and Constantin Job 

IMR Division of Auburn International, Inc. 

4473 Willow Road, Suite IZ5 

Pleasanton, California 64566 

Industrial Magnetic Resonance (IMR), a new process control 

technique, is defined as magnetic resonance designed for in- 

plant use. An IMR spectrometer is an NMR spectrometer equipped 

with the hardware, software and methodology necessary to control 

a specific industrial process under actual plant conditions. In 

order to be successful, an IMR spectrometer must be able to 

operate in a plant for extended periods of time without operator 

adjustment or intervention. It must also change its own sample 

and make measurements precise enough to control the process 

stream. 

In this talk, we will describe IMR spectrometers used in two 

different industrial applications. One being used to measure the 

moisture content of aluminum oxide as it exits a rotary kiln. The 

other application controls the addition of water to wheat prior 

to its being milled into flour. This process is known as wheat 

tempering and is an essential step in the milling process. The 

spectrometer, which will be described, is light, portable and 

self-calibrating. The complete IMR spectrometer will be 

described, including the sampling system, pneumatic control 

system and the methodology used.

Monday - PM 

NMR for the Detection of Explosives 

William L. Rollwitz, Armando De Los Santos, George A. Matzkanin, 

and J. DerwinKing 

Southwest Research Institute 

Division of Instrumentation and Space Research 

6220 Culebra Road 

San Antonio, TX 78213 

High energy explosives have hydrogen NMR characteristics which are unique 

and include very short values of T, and very long values of T,. These 

characteristics cause problems when NMR is used to detect the presence of high 

energy explosives in baggage, letters, packages, and soils when these items or 

the NMR detection head are moving rapidly. The level crossing technique 

(NMR/NQR) is used to reduce the long T, values of the explosives so that they 

can be detected rapidly. By using the hydrogen NMR signal, the level-crossing 

technique and other discrimination methods it is possible to detect the 

presence of almost all explosives hidden in baggage, letters, packages and 

soils using magnetic fields of less than 0.I Tesla and to discriminate rapidly 

the hydrogen NMR signal caused by the explosives from the hydrogen NMR signal 

from the other hydrogen containing materials that may be present in the 

baggage, mail, packages and soils. It is even practical to consider portal- 

type NMR detection heads to detect the presence of explosives hidden on or in 

people.

Tuesday - AM 

WHY IS SOFTWARE SO HARD? 

A CONTRARY VIEW OF NMR DATA PROCESSING 

Jeffrey C. Hoch 

Rowland Institute for Science 

100 Cambridge Parkway 


New techniques for processing NMR data appear with increasing frequency. 

Noteworthy examples include non-FFT spectral estimates 1-4, symmetry filters s, 

and pattern recognition 6 . Despite the fact that the operations required by these 

methods are often simple, their implementation on a spectrometer can be a difficult 

task. This stands in stark contrast to the ease with which new pulse programs are 

implemented on modern spectrometers. Turn-key NMR software packages, available 

for general purpose computers, provide environments which are somewhat more 

hospitable toward the implementation of new processing methods. Much of this 

flexibility is simply due to the software development tools found on general purpose 

computers, however. 

A software environment for NMR data processing designed explicitly for the 

purpose of providing programming flexibility is described. The goal of this software 

Is to make the implementation of a new data processing program as straightfor- 

ward as the implementation of a new pulse program. Design decisions have been 

made in favor of simplicity rather than performance whenever those two goals are 

in conflict. A toolkit approach has been utilized, in which many small, independent 

programs perform simple operations on a common data structure. The implemen- 

tation of a procedure for performing symmetry recognition on 2D spectra provides 

an illustrative example. 

1. E. Laue, M. Mayger, J. Skilling, and J. Staunton J. Magn. Reson. 68, 14 

(1988). 

2. H. Barkhuijsen, J. DeBeer, W. Bovee, and D. Van Ormondt J. Magn. Reson. 

61, 46s (1985). 

3. J. Tang, C. Lin, M. Bowman, and J. Norris J. Magn. Reson. 62, 167 (1985). 

4. J. Tang and J. Norris J. Chem. Phys. 84, 5210 (1986). 

5. P. Bolton J. Magn. Reson. 70, 344 (1986). 

6. P. Pf/indler and G. Bodenhausen J. Magn. Reson. 70, 71 (1986).

Tuesday - AM 

SELECTIVE DATA SAMPLING: APPLICATION TO 2D NMR 

Ernest D. Laue, Department of Biochemistry, University of Cambridge, 

Tennis Court Road, Cambridge, CB2 I QW, U.K. 

Novel methods for selectively sampling NMR data, e.g. exponential 

sampling 1'2 will be discussed. Such methods are of particular interest 

in 2D NMR where, for reasons of sensitivity, data often have to be 

truncated in the second dimension (tl). Selective sampling, in 

conjunction with methods such as maximum entropy for reconstructing spectra 

from incomplete time domain data, offers a way of obtaining better 

resolution in the second dimension (Wl), for a given recording time. This 

gives an improvement on maximum entropy reconstructions from 

conventionally sampled (but truncated) data 5. 

In exponential sampling, data points are measured with exponentially 

decreasing frequency. When only selected time domain data points are 

recorded, the data processing in effect both extrapolates beyond and 

interpolates between the measured points. Exponential sampling is 

applicable to exponentially decaying data which is cosine modulated in t I. 

For different data, alternative sampling schemes would be possible. 

I. 

. 

. 

Such methods might also be of use in other areas, such as NMR imaging. 

J.C.J. Barna, E.D. Laue, M.R. Mayger, J. Skilling and S.J.P. Worrall, 

Biochem. Soc. Trans., 1986, 14, 1262. 

J.O.J. Barna, E.D. Laue, M.R. Mayger, J. Skilling and S.J.P. Worrall, 

J. MaKn. Reson. in press. 

E.D. Laue, M.R. Mayger, J. Skilling and J. Staunton, J. 

Reson., 1986, 68, 14. 

EDLmc ? 

12 January, 198'/

Tuesday - AM 

Pattern Recognition in High-Resolution 2D NMR Spectra : 

A Closer Look at Cross-Peaks. 

Peter Pf'~ndler, Marjana Novi~', Hartmut Oschkinat, Steve Wimperis, 

Guy Jaccard, Urs Eggenberger, Dominique Limat and Geoffrey Bodenhausen, 

Institut de chimie organique, Universit~ de Lausanne, 

Rue de la Barre 2, CH-IO05 Lausanne, Switzerland. 

In favourable systems, it is now possible to analyze 2D correlation spectra and 

2D double-quantum spectra entirely without human intervention by means of 

pattern recognition procedures. The shifts and couplings can be identified 

regardless of the number of protons in the molecule, provided the coupling 

topology is reasonably simple (current strategies are designed for systems 

where each proton has at most five coupling partners), and provided the effects 

of strong coupling are not too pronounced. Algorithms will be described which 

can handle multiplets in both COSY and double-quantum spectra with essentially 

the same logic, despite of the apparent lack of similarity. Complex multiplets 

can be identified and the relevant splittings can be measured by checking for 

symmetry relationships. 

Structural information can be obtained from 2D exchange experiments with small 

flip angles, where one observes (in addition to COSY-like signals) a variety of 

peaks due to dipolar and other relaxation processes. The analysis of these 

signals allows one to determine the W-matrix of transition probabilities. 

Recently, we have predicted and confirmed experimentally that unusual COSY 

cross-peaks can arise between spins that do not have a mutual scalar coupling. 

These are due to coherence transfer induced by correlated relaxation 

mechanisms. Such anomalous cross-peaks not only present a challenge for pattern 

recognition, but lead us to question some fundamental assumptions used in the 

interpretation of COSY spectra.

Tuesday - AM 

INDIRECT DETECTION OF lSN and 13C: 

INSTRUMENTAL CONSIDERATIONS AND BIOCHEMICAL APPLICATIONS. 

David Cowburn 

The Rockefeller University, 

New York, New York, 10021 

Biochemical applications of NMR are usually limited by sensitivity of detection, and selectivity 

and resolution of signals from individual groups. Indirect detection, via protons, of hetronuclei like ~SN, 

t3C, and 113Cd permit gains of sensitivity of the order of the ratios ~'n/)'x to more than the power of 2, 

and selectivity and resolution are increased by the usual advantages of two-dimensional NMR methods. 

For natural abundence samples, these experiments are especially demanding of instrumental precision 

and stability. Methods for evaluating and improving probe, radiofreqency, and numerical processing 

performance will be described. The various pulse sequences for indirect detection differ in their 

sensitivity to instrumental factors, and choice of sequence should be tailored to application. 

These methods have, however, some apparent disadvantages. Relatively long evolution and 

preparation times may permit excessive transverse relaxation, limiting f~ resolution. For natural 

abundence studies for lSN and ~3C, there is an apparent disadvantage compared to direct detection 

methods with proton decoupling. In indirect detection experiments, the abundent protons' homonuclear 

couplings are superimposed on the spectra, while in more conventional direct detection, the signals are 

decoupled from protons, and show only low intensity homonuclear satellites. These and other apparent 

disadvantages can be alleviated in part by use of Linear Predictive Singular Value Decomposition 

0__,PSVD) analysis, and recombination of filtered roots(I). 

Supported by grants from NSF, and NIH. 

1. Schussheim, A. E., Cowbum, D. 1987 J. Magn. Res., in press.

Tuesday - AM 

Proton-Detected Reteronuclear One- and Two-Dimensional NMR Spectra of 

Biomolecules: Shift Correlation and Relaxation Measurements. 

William M. Westler and ~ohn L. Markley 

Department of Biochemistry 

College of Agricultural and Life Sciences 

University of Wisconsin-Madison 

420 Henry Mall 

Madison, Wisconsin 53?06, U.S.A. 

Indirect detection of a heteronucleus by scalar coupled protons is a 

powerful technique that extends the range of 13C and IsN NMR spectroscopy to 

include samples of limited quantity or solubility. Since the relative 

sensitivity for detection of NMR active nuclei is proportional to the cube of 

the magnetogyric ratio, the maximum sensitivity in a he teronucl ear correlation 

experiment can be obtained by detecting the nucleus with the larger 

magnetogyric ratio in the coupled spin system. The sample requirement for 

proton-detected heteronuclear correlation spectroscopy is at least an order of 

magnitude lower than that for conventional heteronuclear experiments. We have 

collected one- and two-dimensional proton-detected heteronuclear NMR spectra of 

selectively and uniformly ISC and ISN labeled proteins [Anabaena 7120 

ferrodoxin (10,000 dalton); Staphylococcus aureus nuclease (17,000 dalton); and 

Anabaena 7120 flavodoxin (23,000 dalton)]. Two proteins have been studied at 

natural abundance [turkey ovomucoid third domain (6,000 dalton) and summer 

squash trypsin inhibitor (3,000 dalton)]. A promising experiment is one that 

we call "HOTRAT u (_Hydrogen Observation of Transferred RAre _Tl'S). This method, 

which allows one to measure longitudinal relaxation times of rare nuclei in 

samples of limited quantity or solubility, is useful in light of the current 

interest in the dynamics of biomacromolecules. 

[This research was carried out at the National Magnetic Resonance 

Facility at Madison (NMRFAM) and was supported by NIH grant RR 02301.]

Tuesday - AM 

NOVEL APPROACHES TO THREE-DIMENSIONAL NMR 

C. Griesinger, R. Br~schweiler, O.W. S~rensen 

and R.R. Ernst 

Laboratorium fur Physikalische Chemie 

Eidgen~ssische Technische Hochschule 

8092 Z~rich, Switzerland 

Extensions of NMR spectroscopy to three dimensions 

will be described. Useful 3D techniques can be 

obtained by combining building blocks of known 2D 

pulse techniques. In order to achieve tolerable 

sizes of data matrices and measuring times new 

approaches have been developed for the extraction of 

restricted volumes of the 3D spectrum. 

3D NMR presents considerable potential for NMR 

investigations of large biological macromolecules in 

solution where overlap of cross peaks is becoming a 

limiting factor.

Tuesday - PM 

Spatial and Spectral Diffusion of Magnetization 

J. S. Waugh* and C-G. Tang 



I. The spatial diffusion of Zeeman energy in a rigid crystal ("spin 

diffusion") is the simplest experimentally realizable example of a trans- 

port process and is therefore of fundamental theoretical interest. How- 

ever no "proper" experimental measurement has yet been made. We will out- 

line an approach through computational spin dynamics based on a classical 

model. Results will be presented for the magnitude and anisotropy of 

diffusion in a cubic lattice (CaF2) and on a randomly diluted lattice, 

complementing and extending an alternative earlier approach by Lowe and 

Gade. 

2. Two separated resonances which overlap slightly because of dipolar 

broadening are expected to cross-relax to a common spin temperature: the 

expected rate may be estimated from a Gaussian overlap integral. On this 

basis the two components of the Pake doublet in gypsum are expected to 

communicate in timms of the order of seconds. Experiments will be des- 

cribed which show that the actual rate is ~1000 times slower.

Tuesday - PM 

SUPPRESSION OF DIPOLAR BROADENING BY MAGIC ANGLE SPINNING 

Robert A. Wind, Steven F. Dec and Gary E. Maciel 


Colorado State University 

Fort Collins, CO 80523 

We have developed a Magic Angle Spinning system that operates over a 

large range of rotor diameters and corresponding rotor velocities, the 

latter reaching a maximum of 85% of the velocity of sound with air as a 

driving gas, and a maximum of 105% of the velocity of sound (in air) 

using a combination of He and air as driving gases. A spinning system 

with a 4.5-mm o.d. rotor, which can be rotated at a frequency of up to 23 

kHz, has been used to investigate the line-narrowing possibilities of 

abundant-spin spectra in solids via MAS. Results will be shown of 1H and 

19F spectra of a variety of solid compounds with static linewidths 

varying from 12 to 30 kHz. The residual linewidths obtained as a func- 

tion of spinning speed will be discussed, and the prospects of obtaining 

chemical shift information from the narrowed spectra will be considered. 

Finally, results will be shown of 13C spectra obtained via cross polari- 

zation at high spinning speeds.

Tuesday - PM 

DIFFUSION OF SPIN ORDER IN RESOLVED SOLID STATE NMR SPECTRA 

D. Suter 

University of California, Berkeley 

Polarisation of individual spins in a solid is not a constant of motion, 

but gets dispersed over all coupled spins under the influence of the so 

called flip flop terms of the dipole-dipole interaction. In large spin 

systems the process of redistribution of spin order bears the 

characteristics of a diffusion process and is therefore called spin 

diffusion. The rate at which order is tranferred from one spin to 

another depends on the strength of their dipole-dipole interaction and 

therefore contains information about nuclear distances. Other 

parameters influencing the diffusion rate are differences of resonance 

frequencies and couplings to spins that do not participate in the 

exchange process. By measuring the diffusion of different types of spin 

order, it is possible to distinguish between different diffusion 

mechanisms. 

Diffusion of Zeeman - Order Diffusion of Ouadrupolar Order 

Figure: Diffusion of Zeeman and quadrupolar order in a single crystal of 

deuterated malonic acid. 

Reference: 

D. Suter and R.R. Ernst, Physical Review B 32, 5608 (1985).

Tuesday - PM 

WF54 - POSTERS 

2D EXCHANGE NMR IN NON-SPINNING POWDERS 

C. Schmidt, S. Kaufmann, S. Wefing~ D. Theimer~ 

B. Bl~mich" and H. W. Spiess~ 

Max-Planck-Institut f~r Polymerforschung~ 

Postfach 31489 D-6500 Mainz 

Information about molecular motions in isotropic 

solids is typically derived from lineshape analyses of 

wideline NMR spectra~ while in liquid samples 2D exchange 

NMR has become an accepted method. In 2D exchange spectra 

some of the information hidden in the lineshapes of 1D 

spectra is reencoded into frequency coordinates of 

exchange signals~ where it is accessible more accurately 

and in a model-independent fashion. 

We have studied deuteron and C-13 2D exchange NMR 

for the characterization of molecular motions in powders 

and amorphous solid samples. The deuteron quadrupole 

coupling tensor is axially symmetric~ so that particu- 

larly simple exchange signals result. Discrete jumps are 

characterized by elliptical exchange singularitiesp where 

the excentricity of the ellipse is a direct measure of 

the jump angle. Diffusive motions result in homogeneous 

broadening with.characteristic 2D lineshapes discrimina- 

ting different stages of partial diffusion towards the 

full diffusion limit. For short mixing times pure 

diffusion~ diffusion in connection with discrete jumps, 

and pure jump motions can be distinguished. 

The 2D exchange experiment can also be performed in 

C-13 NMR on selectively labelled compounds. The asymmetry 

of the chemical shielding tensor~ however, leads to more 

complicated 2D exchange patterns. Experimental and theo- 

retical data demonstrate that the wideline 2D exchange 

experiment produces a direct image of the jump angle 

distribution. 

References: 

1) C. Schmidt, S. Wefing~ B. Bl~mich and H.~W. Spiess~ 

Chem. Phys. Left. 130, 84 (198b). 

2) M. Linder, A. H~hener and R. R. Ernst~ J. Chem. Phys. 

73~ 4959 (1980).

Tuesday - PM 

WKI4 - POSTERS 

SYMMETRY AND ANTISYMMETRY IN 2D NMR SPECTRA 

O.W. S6rensen, C. Griesinger, C. Gemperle 


Laboratorium f~r Physikalische Chemie 

EidgenSssische Technische Hochschule 

8092 Z~rich, Switzerland 

The conditions for obtaining 2D spectra symmetric or 

antisymmetric with respect to reflection about the 

diagonal have been extended and generalized. They 

can be formulated either in terms of the structure 

of pulse sequences or in terms of the coherence 

transfer pathways selected. 

Recent results indicate that new experimental 

techniques producing antisymmetric or asymmetric 2D 

spectra can be of advantage in certain practical 

situations. For example, experiments leading to 

antisymmetric spectra often result in suppression of 

uninformative and disturbing diagonal peaks.

Tuesday - PM 

WKI2- POSTERS 

QUANTITATIVE INTERPRETATION OF A SINGLE 2D NOE SPECTRUM 


AT&T Bell Laboratories 

Murray Hill, NJ 07974 

A new method is suggested for the quantitative in- 

terpretation of 2D NOE data using selective relaxation rates 

and matrix techniques. This approach reduces the experimen- 

tal time from one week to one day, gives proton-proton dis- 

tances with a precision of 10.1 A, and can be used to 

characterize the internal dynamics. With this approach the 

structural and dynamic properties of Gramicidin S were 

determined from a single 2D NOE spectrum with a mixing time 

of 0.2 s. The peak volumes in the 2D experiment were scaled 

via the measured selective relaxation of Phe NH and Orn 

protons and the matrix of scaled peak volumes was solved to 

yield the relaxation rate matrix. The distances measured by 

this approach were indistinguishable (~0.1 A ) from those 

measured from 1D NOE experiments, the buildup of cross peaks 

in the 2D NOE experiments, and the distances expected from 

the crystal structure. The dynamics were determined from 

the ratio of the sum of all the cross relaxation rates to 

the rate of decay of the diagonal peak which, for isotropic 

motion, depends only the the correlation time. This 

analysis showed a correlation time for the NH and H ~ protons 

of 0.9~0.1 nsec; the close correspondence between the ob- 

served and expected values show that the peptide backbone is 

rigid in solution over the time scale of molecular tumbling. 

Internal motions of make a significant contribution to the 

relaxation of some side chain groups. The implications and 

limitations of this approach and the applications to DNA 

structure determination will be discussed.

Tuesday - PM 

WK22 - POSTERS 

SOLVENT SUPPRESSION WITHOUT PHASE DISTORTION 

Malcolm H. Levitt* and Mary F. Roberts 

M.I.T., NN14-5122, Cambridge, MA 02139 

Ve describe a new class of pulse sequences, NERO (Non-linear Excitation 

Rejecting 0n-Resonance), which allow wideband excitation of an 

spectrum except for a deep, flat section near the carrier where the 

response is zero. The novel feature of the new sequences is that phase 

distortion of excited resonances is negligible, in contrast to usual 

methods based on linear response. Ve will show numerical simulations 

and experimental results for the following sequence, called NER0-1: 

D B N 

120°-~1-115°-T2-115 °-2~3-115"-~2-115 °-~1-120°-~ r 

where pulses 180 ° out of phase have an overbar, and delays ~k are given 

by 

~1 = 0" 139/(~exc/2n) 

~2 = O. 625/( ~exc/2 n) 

2~ 3 = 0.428/(~exc12n ) 

~r = 0"222/(~exc/2n) 

Here (~exc/2n) is the offset frequency (Hz) of the center of the 

excited spectral region. This class of pulse sequence is capable of 

providing solvent suppression almost free from undesirable phase 

distortions.

Tuesday - PM 


FLOW IMACINC 

C. L. Dumoulln*, S. P. Sou=a, H. R. Hart Jr. 

Ceneral Electric Research and Development Center 

P0 Box 8, Schenectady, New York 12301 

Many flow sensitive NMR procedures have been proposed and demonstrated. 

All of these methods rely on either longitudinal magnetization or transverse 

magnetization for flow discrimination. Time-of-flight and spin washout are 

examples of flow sensitive techniques which make use of longitudinal magneti- 

zation. In these methods, the longitudinal magnetization is changed in one 

location and monitored in another downstream from the first. Techniqdes which 

make use of transverse magnetization such as the one described below typically 

monitor the phase of spin magnetization and thus are not constrained by the 

geometry of flow. 

The most significant problem in blood flow imaging in animals or humans 

is the suppression of signals arising from non-moving spins. This is a par- 

ticularly severe problem because blood vessels are relatively small when com- 

pared to the volume of the surrounding tissue and blood flow is usually pulsa- 

tile rather than constant. The rapid-scan, phase contrast technique presented 

here circumvents these problems and has proven very useful in obtaining non- 

invasive angiograms of healthy and diseased patients. 

The flow-induced phase shift of a hi-polar gradient pulse is simply 

- ~VTA G 

where • is the flow-induced phase shift, 7 is the gryomagnetic ratio, V is the 

component of spin velocity in the direction of the applied magnetic field gra- 

dient, T is the time between the centers of the lobes of the bipolar gradient 

and A G is the area of the first lobe in the bi-polar pulse (the area of the 

second lobe is -AG). To selectively detect flow in an imaging or spectroscopy 

procedure one can simply acquire two sets of data under different conditions 

of V, T or A G. We have found that the inversion of the bi-polar gradient 

pulse gives the best results. Thus, two echoes are obtained, one with 

- 7VTA G and the other with ~ - 7VT(-Ac). Moving spins are selectively 

detected and stationary spins suppresse~ by taking the difference of the two 

echoes. Since the flow sensitivity of such a procedure is only in the direc- 

tion of the applied field gradient, two flow images are obtained with orthogo- 

hal flow sensitivities and combined to give the total flow image. The inten- 

sity of each pixel in the image is a quantitative measure of flow provided the 

flow-induced phase shift, #, is less than about I radian. 

Suppression of non-moving spins can be enhanced by a weak dephasing gra- 

dient applied in the direction of the image projection. Such a gradient 

dephases spin magnetization over the large volume of non-moving spins and has 

little effect in the relatively small vessels. Additional suppression can be 

obtained by acquiring data very quickly and with short pulse-to-pulse inter- 

vals. Rapid scanning saturates non-moving spins while spins which move into 

the detection region are fully relaxed. Fast scanning also makes the flow 

imaging procedure much less sensitive to patient motion since differences of 

data acquired in very short intervals are taken.

Wednesday - AM 

SURFACE-SELECTIVE NMR BY DYNAMIC NUCLEAR POLARIZATION 

EXPLORATION AT THE POLYMER INTERFACE 

H. Seidei, l" R. D. Kendrick and C. S. Yannoni 

IBM Almaden Research Center, San Jose, CA 

and 

M. E. Galvin 

AT&T Bell Laboratories, Murray Hill, NJ 

One of our primary motivations for initiating a program in solid state NMR of 

dynamically polarized nuclei is the belief that this can be a useful new method for the 

study of structure and dynamics of molecules at surfaces. To explore this possibility, 

we have built a 60 MHz DNP-NMR spectrometer based on an electromagnet probe 

which uses a quasi-optical (Fabry-Perot) cavity to pump the ESR at 40 GHz. l 

Although DNP has traditionally been viewed as a means for obtaining high nuclear 

polarization, °" the spatial selectivity of DNP will be emphasized here. We intend to use this 

selectivity to preferentially polarize nuclei in molecules near the surface of a material 

which contains unpaired electron spins. The selectivity arises from the dependence of the 

Overhauser enhancement on the inverse sixth power of the electron-nuclear distance. 

Generally, since the sample will be in the bulk form commonly used in NMR 

experiments, the surface will be internal i.e. interfacial regions between the material of 

interest and the material containing the source of unpaired spins. As a demonstration 

of the efficacy of this approach, we will discuss results obtained in a composite of 

polyacetylene in polyethylene. 3 This polymer composite provides not only a reasonable 

spin dynamical model for a molecule (polyethylene) at the surface of a "metal" particle 

(polyacetylene), 4 but also introduces the possibility of using DNP-NMR as a tool for 

studying intimacy of mixing in polymer blends, one component of which contains 

unpaired spins. We have observed 1H as well as IH-decoupled carbon-13 spectra for this 

material, with and without DNP, using both thermal and cross polarization. The results 

indicate that selective NMR spectra of polyethylene carbons in the interfacial regions can 

be obtained. 

Since the unpaired electron spins responsible for the polarization are confined to very 

small island structures (

. 

. 

. 

4. 

-2- 

D. J. Singel, R. D. Kendrick and C. S. Yannoni, 26th ElqC, April 1985, Asilomar, 

California; R. D. Kendrick, H. Seidel, D. J. Singel and C. S. Yannoni (manuscript 

in preparation). 

We have recently achieved very large 13C polarization via the Overhauser effect in 

a one-dimensional organic charge transfer conductor with a narrow ESR spectrum 

("30 milligauss width) which has permitted o~ervation of 1016 carbon-13 spins with 

a single pulse at room temperature after a 1-second polarization period "High 

Resolution DNP-NMR and Knight Shift Suppression in a One Dimensional Charge 

Transfer Conductor"; R. D. Kendrick, H. Seidel, D. J. Singel, W St6cklein" and C. 

S. Yannoni, poster to be presented on Monday, April 6 at the 28th ENC. 

M. E. Galvin and G. E. Wnek, Polymer 23, 795 (1982). 

In the trans form present in these composites, polyacetylene is a semiconductor 

containing unpaired electron spins which exhibit-fast one-dimensional diffusion. 

This leads to an Overhauser enhancement of the kind one might expect from a 

metal: M. Nechstein, F. Devreux and R. L. Greene, Phys. Rev. Lett, 44, 356 (1980); 

M. Manenschijn, M. Duijvestijn, J. Smidt, R. A. Wind, C. S. Yannoni and T. C. 

Clarke, Chem. Phys. Lett. 112, 99 (1984). 

5. M.E. Galvin, dissertation, Massachusetts Institute of Technology (1984).


~FIFTY-FOUR-FORTY OR FIGHTI" l 

High-speed IH MAS-NNtR of Inorganic Solids 

and Paramagnetic Compounds 

James P. Yesinowski," Hellmut Eckert, and Akbar Nayeem 

Division of Chemistry and Chemical Engineering 

California Institute of Technology 

Pasadena, CA 91125 

High-resolution IH 1V[AS-N1VIR spectra of solids have generally been obtained 

using multiple-pulse line-narrowing techniques (CRAMPS) or isotopic dilution with 

deuterium to reduce the strong homonuclear dipolar interactions. We will show exper- 

imental results from 1H MAS-NMR at 200 and 500 MHz indicating that high speed 

spinning alone (at ca. 8 kHz) results in high-resolution spectra for many inorganic 

solids and minerals. Even in cases where the homonuclear dipolar coupling greatly 

exceeds the spinning speed, the inhomogeneous character of the interaction can result 

in sharp spectra with many spinning sidebands. Experimental considerations will be 

discussed, and examples of structural characterization in minerals, glasses, and cal- 

cified tissue such as bone and teeth will be given. The correlation of the isotropic 

proton chemical shift with the strength of hydrogen-bonding will be discussed, and 

correlated with 2H NMR results. 

The MAS-NMR of paramagnetic compounds is another area of interest. We will 

demonstrate that high-resolution IH MAS-NMR spectra of paramagnetic transition- 

metal compounds can be obtained. As a consequence of the electron-nuclear dipolar 

coupling such spectra exhibit intense spinning sidebands extending over tens or hun- 

dreds of kilohertz. We will discuss the theoretical treatment developed to account for 

the spinning sideband intensities and the peak shape, which includes the effect of the 

electron g-anisotropy. 

IThis bellicose slogan was the rallying cry of supporters of James Polk in the U.S. Presidential 

election of 1844. It referred to the disputed northern boundary of the Oregon territory, which 

expansionist Americans wanted set at a latitude of 54040 ', within 5' of the magic angle. This slogan 

is thus still relevant for solid-state NMR spectroscopists in their daily fight for increased resolution.


THE DETERmiNATION OF THE STRUCTURE OF PARTIALLY-ORIENTED SOLIDS 

USING 2D-MAGIC-ANGLE-SPINNING N}~ 

Gerard S. Harbison 

Department of Chemistry, SUNY Stony Brook, Stony Brook, NY 11794. 

V.-D. Vogt, C. Boeffel, B. Bluemich and H.W. Spiess 

Max-Planck-Institut fuer Polymerforschung, Postfach 3148, D-6500 Mainz, FRG. 

High-field magic-angle-spinning (MAS) spectra of oriented samples display 

variations in the phases and intensities of the MAS centerbands and sidebands, 

which depend on the position of the sample order axis about the rotor axis at 

the time the precession of the nuclear magnetization begins. This phenomenon 

may be observed by synchronizing the spectral excitation with the sample 

rotation (I), and we have shown (2) that it may be made the basis of a 2D-NMR 

experiment, in which the first time dimension is the (time-dependent) rotor 

position, and the second is routine unrestricted acquisition. The 2D spectra 

thus obtained consist of MAS centerbands and sidebands in two dimensions, 

whose intensities depend on the size of the chemical shielding tensor, its 

orientation relative to the sample order axis, and the degree of disorder of 

the sample about that axis. Using a spherical harmonic expansion of the 

shielding tensor orientation about two Euler angles in the frame of reference 

of the order axis (3), we can, without recourse to model-building, determine 

the complete orientational distribution function of the residue in question 

relative to the sample axis. Thus, for each distinct, resolvable resonance in 

a complex sample, we can determine the preferred orientation of that residue, 

and its statistical distribution about that preferred orientation. Obviously, 

determining these quantities for a real sample, coupled with the geometrical 

restrictions imposed by the laws of chemistry, is tantamount to determining 

its structure on the atomic scale. 

We have applied our experimental and theoretical protocols to a number of 

oriented polymers, among them polyethylene terephthalate (PET) and several 

liquid-crystalline polymers. We shall illustrate their use with a discussion 

of the structure of the crystalline and amorphous phases of PET, in which the 

results obtained by our method are in close agreement with existing x-ray 

studies. We shall also consider their potential application to other systems. 

(1) M. blaricq & J.S. Waugh (1979) J. Chem. Phys. 70:3300 

(2) G.S. Harblson & H.W. Spiess (1986) Chem. Phys. Lett. 124:128 

(3) G.S. Harbison, V-D. Vogt & H.W. Spiess (1987) J. Chem. Phys., in press.


MULTIPLE PULSE ECHO TRAINS 

IN 

ROTATING SOLIDS 

A.C. KOLBERT, D.P RALEIGH, M.H. LEVITT, and R.G. GRIFFIN 

Francis Bitter National Magnet Laboratory 

and 



Cambridge, MA 02139 

One of the most useful and pedagogically important pulse 

NMR experiments is the Hahn spin echo. Today this experiment is 

employed extensively in NMR imaging and an understanding of the 

basic principles of echo formation permits an understanding of a 

large variety of other phenomena in magnetic resonance. The 

importance of echoes has provided the impetus for us to 

investigate the effects of ~ pulses and K pulse trains in magic 

angle sample spinning experiments, particularily in the slow 

spinning regime. We first review the effects of a single and two 

pulses on rotational echo trains and then discuss a number of 

interesting new effects. These include a new class of multiple 

pulse trains, the effects of r.f. phase shifts on the phases of 

the echo train, and a combination of both. In addition, we will 

also describe a 2D version of one of the experiments which may 

prove useful in measuring small shift anisotropies.


Field Cycling NMR as a Tool for NQ~RSpectroscopy of Weakly 

Quadrupole-Coupled Nuclei: Pyridine, Imidazole, and the 

Nucleosides Adenosine, Guanosine and Inosine. J. L. Ragle, 

Department of Chemistry, University of Massachusetts, 

Amherst, MA 01003. 

NMR experiments which cycle with B ° or Brf have been used 

for over 3 decades for various purposes. In the case of 

integer spin nuclei and in the weak quadrupole coupling 

regime, very high resolution zero field spectra may be 

obtained in either the time or frequency domain by several 

of these techniques. 

This talk discusses use of the simplest of these, adiabatic 

field cycling between high field and zero field, to measure 

NQR spectra in several sets of molecules: imidazole and 

imidazolium salts, and three nucleosides. Quadrupole 

coupling constants will be discussed in the light of 

structures and MO calculations on these species.


APPLICATIONS OF ZERO FIELD NMR TO THE STUDY 

OF SOLIDS AND LIQUID CRYSTALS 

Ann M. Thayer* 


Time domain zero field NMR methods provide a means of obtaining 

high resolution spectra of polycrystalline or amorphous materials. 

Recent experiments will be discussed which include the observation of 

small motionally induced asymmetries in dipolar coupled systems. From 

such observations, one can obtain a measure of small amplitude libra- 

tional motions or the onset of biaxiality in smectic liquid crystalline 

phases. In addition, experiments involving the use of pulsed dc 

magnetic fields in zero field will also be presented. The behavior of 

a nuclear spin system can be coherently manipulated and probed in zero 

field with dc magnetic field pulses which are employed in a similar 

manner to radiofrequency pulses in high field NMR experiments. DC 

pulse sequences can be used as composite pulses for increased spatial 

homogeneity and for selectivity between isotopic species. 

*Present Address: AT&T Bell Laboratories 

Hurray Hill, New Jersey


Applications of Solid State NMR Methods to 

Problems of Interest to Surface Chemistry 

by 

Paul D. Ellis, Paul D. Majors, ~ Thomas E. Raidy, 2 Paul S. Marchetti, 

Alan Benesi, 3 Doug Morris and Shelton Bank, W and Richard Adams 


University of South Carolina 

Columbia, South Carolina 29208 

For the past several months our group has been interested in the ap- 

plication of multinuclear solid state nmr methods to surface chemistry. These 

problems include studies of simple amines, via 2H and ~SN nmr s'6 on Y-alumina. 

The purpose of these studies is to probe the number of acid sites on the sur- 

face and to extract via indirect methods the surface distribution of AI 3+ 

atoms on Y-alumina. If the experimental gods are willing we will also discuss 

our attempts at the direct observation of th~ A1 s+ distribution via 2~AI nmr. 

Additional studies have involved 9SMo nmr of Molybdenum-Alumina Hydrodesul- 

furization catalysts. Our work is only beginning with these systems, but we 

will summarize our work to date. The work summarized here has been supported 

by the NSF through CHE 86-11306. 

I. Current Address: Lovelace Medical Foundation, Research Division, 2425 

Ridgecrest Dr., SE, Albuquerque, NM 87108. 

2. Current Address: General Electric Co., NMR Instruments, Fremont, CA 

94539. 

3. Current Address: Department of Chemistry, Penn State University, 

University Park, PA 16802. 

4. On Sabbatical leave from SUNY, Albany. 

5. P.D. Majors, T.E. Raidy, and P.D. Ellis, J. Amer. Chem. Soc., 108, 8123 

{1986). 

6. P.D. Majors and P.D. Ellis, ibid, in press.


Quadrupole Nutation NMR. NQR in the Rotating Frame 

W. S. Veeman, R. Janssen, E. Tijink, A. P. M. Kentgens 

Department of Molecular Spectroscopy, Faculty of Science 

University of Nijmegen, Toernooiveld, 6525 ED NIJMEGEN, The Netherlands 

The principle of nutation NMR for quadrupolar spins in solids 

will be outlined. Various applications of nutation NMR for 23Na in 

zeolites, aluminates and silicates will be shown, at room 

temperature and at higher and lower temperatures. 

The combination of rotary echoes with nutation NMR makes it 

possible to demonstrate the existence of fast relaxation processes in 

the rotating frame, related to dynamical processes in the above 

mentioned materials.

Notes

Thursday - AM 

AN OVERVIEW OF SPATIALLY LOCALIZED SPECTROSCOPY 

by 

D.I. Houit 

Biomedical Engineering and Instrumentation Branch 

Division of Research Services 

Building 13, Room 3W13 

National institutes of Health 

Bethesda, Maryland 20892 

Obtaining spectra from a localized region is a difficult task which is 

further complicated by a number of practical problems which defy easy 

solution. The actual act of localization is accomplished with the aid 

of gradients in the B 0 and/or B 1 fields in concert with a variety 

of selective pulses and cycling schemes. However, as the volume of 

interest may be small in comparison to the volume which is capable of 

generating signal, suppression of the latter must be excellent, leaving 

very little room for experimental imperfection. When one considers 

that the sample i5 often alive and may move, that switched-field 

gradients may leave residual eddy currents which generate changing 

fields during data acquisition, that shimming may be well-nigh 

impossible if the volume is remote from the origin of the shim coil set 

and that several transmitting and/or receiving coils may be needed, a 

headache of royal proportions is clearly made manifest. Thus the talk 

will outline in more detail the origins of the- problems, and briefly 

summarize progress made in solving them.

Thursday - AM 

Gradient Transient Effects in Large Bore MR Imaging Systems 

G. H. Glover 

Applied Science Laboratory 

General Electric Medical Systems 

P.O. Box 414, W875 

Milwaukee, WI 53201 

The measured temporal response of the field excited by a whole body MR imaging gradient is 

found to differ from the exciting current. The error field derives from eddy currents induced 

in the magnet and cryostat, and from interactions with the shim coil and their power supplies. 

The impulse response of this spurious field in an Oxford one meter bore magnet can be 

approximated by_B(t,r) = Bo (t) + ~ (t) • 7, where Bo(t) is a spatially invariant transient 

component and G(t) is a linear gradient transient whose direction parallels the exciting 

gradient. The field errors degrade performance and can induce artifacts in imaging sequences 

by causing poor selective excitation and by creating unintentional dephasing during 

evolutionary periods. The effect of spurious gradient transients on imaging sequences is 

examined and examples are given. 

An NMR technique for measuring B(t) is presented. The technique uses two small probes to 

sample the field in two locations following application of a gradient pulse. Analysis of the 

data shows that Bo(t) and G-(t) can be adequately represented as a superposition of several 

exponential processes with time constants from a few msec. to several minutes. 

Correction techniques are presented for cancelling both G(t) and Bo(t). The former correction 

is effected by appropriately modifying the gradient coil excitation current, while Bo 

compensation is obtained by actively driving the Zo shim coil. Adjustment of these filters is 

facilitated by software which calculates the required coefficients from the measured B(t). 

Application of these techniques is found to provide reductions by factors of the order of 50 in 

the spurious response, which is deemed adequate for most present imaging and spectroscopy 

sequences. 

Finally, the use of actively shielded gradient coils for large bore MR systems is discussed. 

Results indicate field reduction by factors of 10-20. When combined with compensation 

techniques, these coils thus yield essentially ideal performance.

Thursday - AM 

IMAGE GUIDED LOCALIZED NMR SPECTROSCOPY AT 1.5 T 

Peter R. Luyten and Jan A. den Hollander 

Philips Medical Systems, P.O. Box I0000, NL-5680 DA Best, 

The Netherlands 

We have explored localization techniques to obtain high 

resolution spectra of human tissues in situ on a 1.5 T whole body 

MR imager. These techniques use switched field gradients to 

define one or more volumes of interest from which NMR spectra can 

be obtained. By using gradients for volume selection the exact 

coordinates of the selected volumes can easily be determined from 

a standard NMR image. 

For optimal results different nuclei may require different 

pulse sequences, in order to meet the typical NMR characteristics 

of each particular nucleus. To obtain localized IH spectra we 

use a technique in which magnetization in the volume of interest 

is retained along the z axis, wheras all signal outside this 

volume is dephased in the xy plane. The advantage of this 

technique is that it allows for localization in one single shot. 

This can be used for shimming the volume of interest. When this 

technique is combined with an appropriate phase cycling scheme a 

very good suppression of unwanted signal from outside the volume 

of intererest is achieved. The disadvantage is that the 

technique relies on relatively long T2 values and small homo 

nuclear J couplings. Therefore, localized 31P spectra have been 

obtained by a different localization technique which avoids 

transversal magnetization during the localization pulse sequence. 

In stead, selected volumes are obtained by using selective 

frequency modulated inversion pulses in combination with an 

appropriate add-subtract scheme. 

Both localization sequences can be easily combined with 

established pulse sequences to measure relaxation rates or to 

perform water suppression and spin editing techniques. Some 

results that were obtained with these techniques and the 

technical difficulties that may be encountered in these 

experiments will be discussed.

Thursday - AM 

PULSE SHAPING FOR TWO-DIMENSIONAL AND MULTIPLE 

PULSE SPECTROSCOPY 


Department of Chemistry, Princeton University, Princeton, NJ 08544 

Applications of shaped radiofrequency pulses to solvent 

suppression in COSY spectra, excitation of two separate resonance 

frequencies, and uniform spin-1 excitation will be presented. We will 

also experimentally demonstrate the tradeoffs between symmetric 

amplitude modulation, asymmetric amplitude modulation, and 

simultaneous phase/amplitude modulation. Recent results of new 

analytical solutions to the Bloch equations, derived for atomic laser 

spectroscopy, will also be experimentally tested. 

I will discuss the tradeoffs between different approaches to 

computerized pulse shape optimization, and show the importance of 

including spectral information to refine shapes. Examples from 

magnetic resonance imaging, high resolution NMR, and perhaps even 

(gasp) laser spectroscopy will be included.

Thursday - AM 

COHERENCE AUGMENTATION BY LIMITING 

THE ENTROPY IN CATALYTIC HYDROGENATION 

Daniel P. Weitekamp 

Arthur Amos Noyes Laboratory of Chemical Physics 

California Institute of Technology 127-72 


The small equilibrium population differences between nuclear spin 

energy levels at ambient temperatures restrict the size of NMR signals to less 

than 10 -4 of their theoretical maxima. Such well-known methods of signal 

enhancement as the Overhauser effect, ClDNP, and optical nuclear 

polarization create large nonequilibrium nuclear magnetizations by taking 

advantage of the coupling to unpaired electron spins. This talk will present 

a fundamentally different approach to very large nonequilibrium 

polarizations, which may be viewed as a coupling of nuclear spins to 

rotational population differences through chemical reaction. 

A consequence of the symmetrization postulate of quantum mechanics is 

that in molecules with equivalent nuclei there is a strict correlation between 

nuclear spin state and rotational state. In molecular hydrogen the even 

rotational states have the singlet nuclear spin wavefunction (para-H2) and 

may be prepared as a low-entropy room-temperature chemical reagent. 

Symmetry-breaking molecular addition of para-H2 results in highly J- 

ordered spin states in the product molecule, which upon rf irradiation give 

rise to extremely large NMR signals. 

The apparatus1 built to perform such reactions in the spectrometer will 

be described. Experimental results at ambient temperatures show 

enhancements of at least several hundred relative to equilibrium signals for 

products and intermediates of homogeneous hydrogenation catalysis. 

These results will be compared with the predictions of the density operator 

theory of this phenomenon2 modified to include relaxation effects. 

1. C.R. Bowers and D. P. Weitekamp, in preparation. 

2. C. R. Bowers and D. P. Weitekamp, Phys. Rev. Lett. 57, 2645 (1986).

Thursday - AM 

ACTIVE SHIELD MAGNETS 

FOR MAGNETIC RESONANCE IMAGING 

David E. Andrews, Ph.D 

OXFORD SUPERCONDUCTING TECHNOLOGY 

600 Milik Street 

Carteret, New Jersey 07008 

Clinical installations of magnetic resonance imaging and spectroscopy 

systems must contend with the interaction of the magnet with its environment. 

In particular, the fringe field of the magnet can restrict choices of 

acceptable sites or require cumbersome and expensive steel shielding. A new 

class of magnets, termed Active Shield magnets, solve this problem. Active 

Shield magnets consist of a novel solenoidal coil configuration which includes 

counter running currents to cancel the fringe field. Design principles, 

performance specifications and economic considerations will be discussed.

Poster Session 

M 

2:00- 5:00 

Mondayj April 6j 1987

o 

u 

i.Z 

o 

Kiln - Poster Session Layout 

WK8 

Flynn 

MK7 

Fesik 

WK6 

Fesik 

MK5 

Davis 

WK4 

Brown 

MK3 

Borgias 

WK2 

Bogusky 

MK1 

Baum 

MK9 

Takegoshi 

WKIO 

McLennan 

MK11 

Poulsen 

WK12 

Mlrau 

MK13 

Holak 

WK14 

Seranaen 

MK15 

Rooney 

WK16 

Hiyama 

Chalkboard 

WK24 

Surer 

MK23 

Sklenkar 

WK22 

Levlttl 

MK21 

WK,?.O 

Ziessow 

MK19 

Yu 

WK18 

Narula 

MK17 

Wang 

MK25 

Ackerman 

WK26 

Barker 

MK27 

Nelson 

WK28 

Brown 

MK29 

Darba 

WK30 

Grahn 

MK31 

Hoch 

WK32 

Johnson 

WK40 MK41 

Warren Bowers 

MK39 WK42 

Ohuchi Bodenhausen 

WK38 MK43 

Mao Boyd 

MK37 WK44 

Bermel Coxon 

WK36 MK45 

Tang Jue 

MK35 WK46 

Stephens Meyerhoff 

wK~ MK4Z 

Picart Pearson 

MK33 WK48 

Craig Rance

Firelight Forum - Poster Session Layout 

WF10 

Chu 

MF9 

Williamson 

WF8 

Pines 

MF7 

Eckert 

WF6 

Kay 

MF5 

Pekar 

WF4 

Lamb 

M_E_3_ 

Gonen 

WF2 

LaMar 

MF1 

Allen 

MF11 

Be.shah 

WF12 

Bork 

MF13 

Bryant 

WF14 

Bryant 

MF15 

Carduner 

WF16 

Duncan 

MF 17 

Earl 

WF18 

Dec 

MF19 

Jiang 

WF20 

Jakobsen 

WF30 

Nissan 

MF29 

Merrill 

WF28 

Wind 

MF27 

Quinting 

WF26 

Limbach 

MF25 

Hill 

WF24 

Campbell 

MF23 

Gleason 

WF22 

Hartzell 

MF21 

Garbow 

MF31 

Oldfield 

WF32. 

Opella 

MF33 

Roberts 

WF34 

Simonsen 

MF35 

Stebbins 

WF36 

Vander- 

Hart 

MF37 

Williams 

WF38 

Lock 

MF39 

St6cklein 

WF40 

Jarvie 

Chalkboard I 

MF51 

Kopelevich 

MF49,~ WF52 

Ronemus Maple 

WF% =~ 

Muir Jarret 

MF47[I WF54 

Nicholson IE]lOmlch 

WF46 N MF55 

Beshah Johnston 

MF45, H WF56 

Brandes Mattingly 

WF44 H MF'57 

Santini Bendall 

MF43H WF58 

Johnson Black- 

ledge 

w% 

Hornak Briggs 

MF41 I"1 WF60 

Behlingll Thoma 

Kormos Lowe 

MF0'IIW 

Keller Hetherington 

James Mateescu 

Schmalo Karczmar 

brock 

Geoffrion Matsui 

MF6511WF76 

Garwood Metz 

v_E_~ I MF" 

Dumoulin Miller 

MF~IWF~8 

Dixon Saarinen 

WF62 H MF79 

Cockman Warren 

MF'IlIWF 

Brown, Szeverenyi 

Women's Rm Men's Rrn 

(J 

03 

P 

LL 

0 

o

MF01 

MF03 

MF05 

MF07 

MF09 

MFll 

MF13 

MF15 

MF17 

MF19 

MF21 

MF23 

MF25 

MF27 

MF29 

Presenter 

Allen, L. 

Gonen, O. 

Pekar, J. 

Eckert, H. 

Williamson, K. L. 

Beshah, K. 

Bryant, R. G. 

Carduner, K. R. 

Earl, W. L. 

Jiang, Y. J. 

Garbow, J. R. 


Monday, April 6, 1987 

Title 

How NMR Studies of Supercritical Fluids 

NMR Spectroscopy Below 1K 

Multiple-Quantum Spectroscopy of Biological Sodium 

51V NMR: A New Probe of Metal Ion Binding in 

Metalloproteins 

NMR of Xenon Absorbed in Solid Polymers: A Probe 

of the Amorphous State 

Tellurium- 125 and Cadmium-111 NMR Study of 

Bonding Properties of Cd(1.x)Zn(x)Te 

Semiconductors 

43Ca NMR In the Solid State 

Phosphorus Poisoning of the Auto Emissions Catalytic 

Converter Studied by 31p NMR 

A Double Quantum Filter for Rotating Solids and 

Some Observations on Labelling in Solids 

An Efficient Stator/Rotor Assembly for Magic Angle 

Spinning NMR 

Solid-State 13C and 15N NMR Studies of Crosslinking 

in Bacterial Cell Walls 

Gleason, K.K. NMR Investigations of Atomic Microstructure 

in Amorphous Semiconductors 

Hill, L. E. 

Quinting, G. 

Merrill, R. A. 

Cesium-133 Solid State NMR of Alkalides and 

Eleclrides 

Multinuclear Solid-State NMR Studies of Derivatized 

Silica Gels 

Magic Angle Spinning of Matrix Isolated Reactive 

Intermediates 

* Location Numbering Scheme: M for Monday, F for Firelight Forum, K for 

Kiln followed by the Poster number. Boldfaced type for featured posters.

MF31 

MF33 

MF35 

MF37 

MF39 

MF41 

MF43 

MF45 

MF47 

MF49 

MF51 

MF53 

MF55 

MF57 

Presenter 

Oldfield, E. 

Roberts, J. E. 

Stebbins, J. F. 

Williams, E. H. 

Sttcldein, W. 

Behling, R. W. 

Johnson, K.M. 

Brandes, R. 

Nicholson, L. K. 

Ronemus, A. D. 

Kopelevich, M. 

Jarret, R. M. 

Johnston, E. R. 

Bendall,. M. R. 

Title 

Second Observation of IH MASS NMR of Lipids and 

Membranes; and 170 Cross Polarization of 

Inorganic Solids 

Increased Resolution for Proton NMR 

Spectra of Solid Materials 

Relaxation Mechanisms and Effects of Motion in 

NaAISi308 Liquid and Glass: A High Temperature 

NMR Study 

A Unique Method for the Quantitative Determination of 

Mixed Liquid and Solid Phases Using Solid-State 

NMR Techniques 

High Resolution DNP-NMR and Knight Shift 

Suppression in a One-Dimensional Charge 

Transfer Conductor 

Acetylcholine Receptor-Agonist Binding. Results 

from Selective Relaxation NMR Experiments 

Design and Use of a Pulse Shaper for High Resolution 

NMR 

The Use of D20 as a Molecular Probe in Determining 

DNA Solid State Packing 

Solid State NMR Studies of IsotopicaUy Labeled 

Gamicidin A in an Oriented Lipid Bilayer 

Solid State 2H NMR Studies of Biphenyl in the 13- 

cyclodextrin Clathrate Complex 

Ultra-High Resolution in IH Spectra at 500 MHz: 

Chlorine Isotope Effects 

Di-13C Labeling: A Means to Measure 12C- 

13C Isotopic Equilibria in the 2-Norbornyl 

Cation 

Dynamic Parameters from Nonselectively Generated 

1D Exchange Speclra 

Calibrated Decoupling of Tightly-Coupled Concentric 

Surface Coils for In Vivo NMR 



1MF59 

MF61 

MF63 

MF65 

MF67 

MF69 

MF71 

MF73 

MF75 

MF77 

MF79 

MK01 

MK03 

MK05 

MK07 

MK09 

MKll 

presenter 

Briggs, R. W. 

Brown, T. R. 

Dixon, T. 

Garwood, M. 

Schmalbrock, P. 

Keller, P. J. 

Lowe, I. J. 

Mateescu, G. D. 

Matsui, S. 

Miller, J. B. 

Warren, W. S. 

Title 

The Cone Coil - An RF Gradient Coil for Spatial 

Encoding Along the B 0 Axis in Rotating Frame 

Imaging Experiments 

An Imaging Method of Shimming for Spectroscopy 

Non-Invasive Spin Labeling of Blood by Adiabatic 

Fast Passage 

NMR Imaging with Extremely Inhomogeneous B 1 

Fields 

Magnetic Resonance Imaging with Phase-Modulated 

Stored Waveforms 

Double Quantum Filtered NMR Imaging: Progress 

Toward Metabolite Specific Images 

A Design of Homogeneous Self-Shielding Gradient 

Coils 

Oxygen- 17 Magnetic Resonance Imaging (OMR.I) 

NMR Imaging Using Circular Signals in the Spatial 

Frequency Domain 

NMR Imaging of Solids with a Surface Coil 

Imaging and In Vivo Spectroscopic Applications of 

Computer Optimized Pulse Sequences 

Baum, J. NMR Studies of ct-Lactalbumin: Char- 

acterization of a Partially Unfolded State 

Borgias, B. A. 

Davis, D. G. 

Fesik, S. W. 

Takegoshi, K. 

Poulsen, F. M. 

Oligonucleotide Structure Ref'mement Based on 

Quantitative 2DNOE Spectra 

Internuclear Distances and Correlation Times from 

Transverse and Longitudinal Cross-Relaxation 

Rates 

Improvements of the 2-D Transferred NOE Experiment 

and Application in the Conformational Analysis of 

Inhibitors Bound to CMP-KDO Synthetase 

A 2D-Exchange Separated Local Field (EXSLF) 

Experiment 

The Structure of the Subtilisin Inhibitor 2 from Barley 

Determined by 1H NMR Spectroscopy, Distance 

Location Numbering Scheme: M for Monday, F for Firelight Forum, K for 


MK13 

MK15 

MK17 

MK19 

MK21 

MK23 

MK25 

MK27 

MK29 

MK31 

MK33 

MK35 

MK37 

MK39 

MK41 

Presenter 

Holak, T. A. 

Rooney, W. D. 

Wang, C. 

Yu, C. 

Zuiderweg, E. R. P. 

Sklenkar, V. 

Ackerman, J. L. 

Nelson, S. J. 

Darba, P. 

Hoch, J. C. 

Craig, E. C. 

Stephens, R. L. 

Bermel, W. 

Ohuchi, M. 

Bowers, C. R. 

Title 

Geometry Calculations and Restrained Molecular 

Dynamics 

2-D NMR - Pseudoenergy Approach to the Three- 

Dimensional Structure of Acyl Carrier Protein 

23Na MR-Invisibility in Living Systems: 2D 

Multiple Quantum NMR and Nutation Dimension 

Effects 

Structures of DNA Oligomers Determined by 2D NMR 

and Distance Geometry Techniques 

Sequential Individual IH NMR Resonance 

Assignments of Cardiotoxin HI from Formosan 

Cobra Venom 

Aspects of Protein Structure Determinations with NMR 

Water Suppression Techniques for the Generation of 

Pure Phase Two-Dimensional NMR Spectra 

Optimization of Quantitative Performance of Spectral 

Analysis by Minimal Sampling 

Quantitation of 1-D Spectra with Low Signal to Noise 

Ratio 

ANALYS2D - Graphics Software for Processing and 

Analysis of 2D NMR Data 

Symmetry Recognition Applied to Two Dimensional 

1H NMR Spectra of Peptides and Proteins 

DISPA-Based Rapid Automated Phasing of FT-NMR 

Spectra 

Networking and Automation in the High-Volume 

Laboratory 

Improvement of Inverse Correlation Experiments by 

Shaped Pulses 

A Partial Excitation Method in Two-Dimensional 

Nuclear Magnetic Resonance Spectroscopy Using 

a Tailored Pulse Having a Sinc Function Shape 

Parahydrogen and Synthesis Allows Dramatically 

Enhanced Nuclear Alignment 



0.* Presenter 

MK43 Boyd, J. 

MK45 Jue, T. 

MK47 Pearson, G. A. 

Mechanisms of Coherence Transfer in Liquids: 

Antiphase and Inphase Transfer 

Simultaneously Observing the Homonuclcar and 

Hctcronuclear Edited Signals without an X 

Nucleus Dccouplcr 

An Improved Chortle Pulse Sequence 



MFI 

FLOW NMR STUDIES OF SUPERCRITICAL FLUIDS 

by 

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


Virginia Polytechnic Institute 

And State University 

B1acksburg, Virginia 24061 

PH (703) g61-5953 

Supercrltlcal (SC) fluids (e.g, CO 2) have become increasing important in 

chromatographic separations. The physical characteristics of these dense 

gases (e.g., hlgh density and low viscosity) a11ow studies of different 

dynamic flow patterns. That is, It is readily possible to vary pressure, 

temperature, and flow rates for SC fluids, thereby, allowing studies of flow 

patterns ranging from laminar to turbulent flow. In addition, previous 

studies in our laboratory I allow accurate mathematical modeling of a given 

flow pattern provtded that spin lattice relaxation (T1) data is known. To 

this end, we have also developed techniques for conveniently measuring (T1'2) 

tn flowing liquids. 

It should also be noted that supercritical fluids are potentially useful 

for studying quadrupolar nuclei (e.g., 14N and 170) and significant 

enhancements in resolution are feasible. That Is, the lower viscosities of SC 

fluids (and corresponding change in correlation times, FC) reduce the 

efficiency of quadrupolar relaxation as recently reported 2. 

In this presentation, we wlll report 200 MHz IHNMR data (including T 1 

relaxation times) for several compounds in flowing supercritical liquids. 

Also various SC flow patterns will be presented and compared with normal 

liquid results. 

1. James F. Haw, Ph.D. Thesis, Virginia Tech, (1982). 

2. Robert, J.M.; Evtlta, R.F.J. Am. Chem. Soc. (1984), 107, 

3733.

MF3- POSTERS 

NMR SPECTROSCOPY BELOW 1K 

Oded Gonen*, P. Kuhns, P. C. Hammel and J. S. Waugh 




L. Boltzmann tells us that large (>104 ) gains in NMR sensitivity can be 

obtained by lowering the temperature to ~YbBo/k, a few millikelvin. We will 

present a selection of results obtained in pursuit of this goal, to illustrate 

the following points: 

>T1, previously expected to be astronomically large, is quite acceptably 

short in powdered samples immersed in liquid 3He. 

>Signals are indeed large: sometimes nearly a volt directly from the 

probe. Monolayers of adsorbed species give strong spectra in a single shot. 

mometer. 

>The shape of the spectrum provides a convenient self-calibrating ther- 

>The usual FT relation between the FID and the spectrum is modified at 

low temperatures. 

>Spin-spin relaxation is sometimes anomalously slow.

MF5 

]dULTIPI, E-QUANT1JN SPECTROSCOPY OF BIOLOGICAL SODIUM 

James pelutr" tad John S. Leigh. Jr. 

Department of" Biochemistry and Biophysics 

University of Pennsylvania 

Philadelphia, Pennsylvania 19104-6089 

In many systems of biological interest, the transverse relaxation of sodium-23 is 

the sum of (at least) two expontatiab. Biexponential relaxation occurs when 

interactions between the nuclear electric qusdrupole moment and fluctuating electric 

field gradients at sodium binding sites cause the "outer" (m - i3/2 ~ m -~1/2) 

trtasitions of the spin-3/2 sodium-23 nucleus to relax fester than the "central" 

( m--1/2 +. re-I/2) transition. Ve have demonstrated that biexponentially-relszed 

sodium can be pessased through a state of deuble-qutatum coherence by • double- 

qutatum filter (1). The filter places the two relaxation components in antiphsse, tad 

yields • signal proportional to the difference between the two components at the end of 

the filter preparation time. 

For on-resontace biexponenthdly-relaxed sodium in an isotropic environment. 

the detected signals for single 90" pulses tad the phase-cycled INADEQUATE double- 

quantum filter ( 90" -T/2 - 180" - X/2 - qO" - 8 - 90" - acquire) are. respectively: 

s(t)me-pus.e" MO (1/5) (3 exp(-t/T~) ,2 exp(-t/T2.)) Ill 

s(t)liltm,ed - M 0 (3/20) (ezp(-~/T2f) - exp(-~/T28)) exp(-SdqS) 

• (exp(-t/T2f) - exp(-t/Tas)) 12] 

Here T2f is the "fast" T 2 of the "outer" transitions. Tax is the "siov" T 2 of the "central" 

transition. Sdq is the transverse relaxation rue of rtak-two deuble-qutatum coherence. 

ud ld 0 is the equilibrium longitudinal sns41netization. 

Because the coherence-trtasi'er experiment is sensitive to differences, rather 

than sums, of the biexpenential decay, it allows more accurate measurement of 

relaxation rates, Indeed. by varying the Utter preparation time. the relaxation rate of 

the "outer" transitions can be indirectly measured (1) even if their decay is fsuter than 

the spectrometer deadtimeT 

Multiple-qutatum ~ may alloy non-invMive discrimination among pools of 

sodium in different physiological compartments. In • laboratory cell suspension, where 

only the intrsceUuhtr sodium relaxed biexponentislly, we have recently demonstrated 

selective detection of intrscelluiar sodium with • double-qutatum filter (2). In more 

complex biologics, systems, the technique of two-dimensional multiple-qutatum 

spectroscopy promises to aid in elucidating both the distribution of sodium among 

dilTerent physiological compartments, and the nature of the spin Hamiltenian in each. 

by highlighting any static qusdrupoiar splittings or dynamic frequency shifts (3). 

Finally, application to other biologically important spin-3/2 nuclei is possible. 

1. j. pek~ and J. S. Leigh. Jr.. J. ~n. Rosen. 69.'582 (1986). 

2. J. pekar. P. F. Rtash.v. and J. S. Leigh, Jr., J. ~n. Rosen., In Press. 1987. 

3. G. Jscard. S. Wimperis, tad G. Bodenhausen, J. Chem. Phys. 85.~2S2 (1986).

MF7 

slV NMR: A NEW PROBE OF METAL ION BINDING 

IN METALLOPROTEINS 

Alison Butler~ Michael Danz|tz~ and Hel]mut Eckert* 

Department o[ Chemistry, University o[ CalJ[ornia at Santa Barbara and Division o[ 

Chem~try and ChemJca/EnE/neering, Ca~/ornia/nstitute o[ TechnoloEy 

High detection sensitivity due to a large magnetic moment, high natural abun- 

dance (99.76 ~) and rapid quadrupolar relaxation in solution render 5iV one of the 

most favorable nuclei for NIVIR studies. In addition, the 51V NMR chemical shifts are 

extremely sensitive to changes in the nature and the symmetry of the ligand coor- 

dination, thereby providing an excellent diagnostic tool for detailed investigations of 

vanadium(V) bonding environments. However, in spite of these advantageous features 

and the fact that vanadium is widely recognized as a biologically important element, 

no 51V NMR data relating to vanadium bound to proteins have been published in 

the literature. In this poster, we report the first 5]V NMR study of a V(V)-protein 

complex: V(V) 2-human transferrin. 

The 11.7T 51V NMR spectrum of a solution containing 2 equivalents of vanadate 

per protein is characterized by two partly resolved resonances at -529.5 and -531.5 

ppm (vs. VOCI3) with a total linewidth of 420 Hz. Linewidths and chemical shifts are 

independent of concentration (range 10 -4 to 10-3M), pH (5-9), nature of the buffer 

solution, and the presence of excess free vanadate. On this basis we assign these reso- 

nances to protein-bound vanadium which is present in two chemically distinct binding 

sites and which is in the limit of slow metal ion exchange on the NMR timescale (2.5, 

10 -4 s). Absolute intensity measurements indicate that the protein-bound vanadium 

is in the slow-motion limit (wrc >> I), and that only the central (1/2 --* -1/2) tran- 

sition is observed. In consonance with this interpretation, measurements at different 

magnetic field strengths reveal the presence of second-order frequency shifts. Several 

examples of the use of 51V NMR to monitor chemical modifications at the binding 

site of V(V)2-human transferrin are discussed.

MF9 

NMR OF XENON ABSORBED IN SOLID POLYMERS 

A PROBE OF THE AMORPHOUS STATE 

Thomas R. Stengle 

Dept. of Chemistry, Univ. of Massachusetts, Amherst, MA 01003 

Kenneth L. Williamson* 

Dept. of Chemistry, Mount Holyoke College, So. Hadley, MA 01075 

Gaseous xenon is readily taken up into the amorphous regions of 

solid polymers. In this state the 12eXe spectrum can be easily 

obtained. In earlier work we have shown that the 120Xe resonance 

is exceptionally sensitive to the nature of its surroundings, 

and that it can be used to probe the structure of liquids and 

lipid bilayers.1 Here we report on its application to the 

amorphous regions of solid polymers. When contained within low 

density polyethylene, the chemical shift of xenon is ca. 200 

ppm downfield from the pure gas. The NMR lines are broad, and 

their shape is especially sensitive to the surrounding 

structure. In particular, the glass transition of polyethyl- 

methacrylate is clearly observed by its effect on both chemical 

shift and lineshape of the xenon signal. The application of 

xenon NMR to several polymers will be discussed. 

IK. W. Miller, N.V. Reo, A. J. M. Schoot Uiterkamp, D. P. 

Stengle, T. R. Stengle and K. L. Wlliamson, Proc. Natl. Acad. 

Sci. USA, 78, 4946 (1981).

MF11 

TELLURI~-I~5 AND CADMIUM-Ill NMR STUDY OF BONDING PROPERTIES 

OF Cd(l-x)Zn(x)Te SEMICONDUCTORS 

K. Beshah, D. Zamir, P. Beola, P. A. Wolff, R. G. Griffin 

G 

Francis Bitter National Magnet Laboratory 


Cambridge. MA 02139 

The ternary alloy Cd(1-x)Zn(x)Te has a zinc blend structure 

whose properties are dependent on the relative composition x. 

Eventhough elaborate theoretical calculations have been done on 

these materials,experimental verifications are scarce. Recently 

EXAFS has been used to verify the bimodal distribution of bond 

lengths in similar alloys. X-Ray diffraction teohnlque averages 

over many unit cells which makes it difficult to probe looallzed 

properties. 

We have applied solid state NMR techniques to determine 

first, second, and third nearest neighbors effect on tellurium 

and o~Imium nuclei from analysis of chemical shifts and linewidths 

of the NMR spectra for various compositions, x. From these results 

we were able to draw conclusions about charge transfer between 

various atoms,the relation between change in bond length and 

chemical shift as a function of x. and existence of clustering. 

The later was determined by comparing intensities of experimental 

data to theoretically calculated spectra assuming random 

distribution.

MF13 

4=Ca NMR In The Solid State 

S. D. Kennedy, S. Swanson, S. Ganapathy, R. G. Bryant 

Department of Biophysics, University of Rocheste~ 

Rochester, New York 14642 

Calcium ion like other group IIA metals has a significant 

nuclear electric quadrupole moment that limits the resolution 

possible in solution phase NMR. The poor resolution becomes 

Norse when the ion interacts with large ligands such as 

proteins which provide a large increase in the correlation 

time for the line broadening interactions. The dynamical 

broadening may be defeated in the solid, but other broadening 

interactions remain that may be defeated by application of 

the appropriate rf fields. The price is signal to noise~ 

since in such odd integral spin spectra narrowed by strong 

proton decoupling and rapid sample rotation at the magic 

angle, the central transition is observed, but usually not 

the others. The signal to noise may be improved 

significantly by exploiting magnetization transfer from the 

protons. Since the ratio of the magnetogyric ratios is 

14.86, the ma>:imum gain is significant. We have observed CP- 

MASS spectra of 4=Ca and found that not only is the 

e~:periment possible, but the spectra obtained hold promise 

for excellent resolution among different calcium sites. This 

poster presents representative CP-MASS calcium spectra, and 

the conditions required to obtain them. Since the contact 

times required for maximum signal are long, and the effective 

gain in the signal strength for the rare spin may be severely 

limited by the decay of the proton magnetization in the 

rotating frame.

MF15 

PHOSPHORUS POISONING OF THE AUTO EMISSIONS 

CATALYTIC CONVERTER STUDIED BY 3xp NMR 

K. R. Carduner* and R. O. Carter III 

Research Staff, Ford Motor Company, Dearborn, Michigan 48121 

ABSTRACT 

Magic Angle Spinning 31p NNR spectroscopy is an informative 

technique for the identification of solid state phosphates. The 

technique is applied to study the extent and chemistry of 

phosphorus poisoning of the three-way catalytic converter (TWC) 

used to control auto emissions. Although it is well-known that 

the source of phosphous is zinc dialklydithiophosphate (ZDPT) oil 

additive, the chemistry of catalysts deactivation is only 

incompletely understood and, as reveiled by the NMR, apparently 

quite complex. NNR of both used and fresh catalysts indicates 

that phosphorus is extraneous to the fresh catalyst and associated 

with the reduced catalytic activity of the aged converter. At 

least three different types of phosphorus compounds are observed 

and identified by the parameters of the isotropic chemical shift 

and chemical shift anisotropy as derived from the envelope of 

spinning sidebands. An overview of isotropic chemical shifts and 

chemical shift anisotropies of condensed phosphates is also 

presented. 

daytime phone 313-337-5454

MFI7 

A DOUBLE QUANTUM FILTER FOR ROTATING SOLIDS 

AND SOME OBSERVATIONS ON LABELLING IN SOLIDS 

William L. Earl" and Beat H. Meier t 

Los Alamos National Laboratory 

Mail Stop C345 

Los Alamos, New Mexico 87545 

For several years we have been investigating the use of 13C labelling in solid samples. 

In our studies of multiple quantum coherence in solids, it occurred to us that it would 

be interesting to use a solid state equivalent of the INADEQUATE experiment to trace 

carbon connectivities. The difficulty with this experiment is that the dipole coupling, 

used to generate the double quantum coherence, changes sign upon sample rotation. Last 

year we demonstrated a pulse sequence which will generate and detect multiple quantum 

coherences in the proton NMR of adamantane with MAS. The logical extension of that 

experiment is a double quantum filter for 13C NMR of a rotating solid. 

We will demonstrate the pulse sequence for such a double quantum filter. Since such a 

filter selects for resonances with a homonuchar dipole coupling, we run into the problem 

of commutation of the dipole coupling tensor with the chemical shift tensor, a problem 

that has been addressed by Maricq and Waugh 1. We will show several 13C spectra which 

demonstrate distortions in the NMR spectrum as a function of the extent of overlap of the 

shift tensors of the dipolar coupled resonances. 

1. M.M. Maricq and J.S. Waugh, J. Chem. Phys. 70, 3300 (1979). 

t Present Address: Laboratorium ffr Physikalische Chemie, ETH-Zentrum, 8092 Zfirich, 

Switzerland.

MFI9 

AN EFFICIENT STATOR/ROTOR ASSEMBLY 

FOR MAGIC ANGLE SPINNING I~R 

by 

Yt Jtn Jtang .1, Warner R. Woolfenden 1, Donald W. Alderman 1, 

Charles L. Rayne 1, Rona]d J. Pugmire 2, and David M. Grant 1 

(1) Department of Chemistry 

(2) Department of Fuels Engineering 

University of Utah 

Salt Lake City, Utah ~I12 

ABSTRACT 

A newlydesigned stator assembly for cylindrical spinners used in 

magic angle spinning nuclear magnetic resonance experiments is 

described. Separate driving and bearing gas chambers allow variable 

and stable spinning speeds and thts design permits easy starting and 

stopping of the rotor. Isolation of the chambers is achieved with the 

application of pressure screws rather than o-rings or glue lines to 

avoid leakage at htgh gas pressures. The overall dimensions are opti- 

mal to facilitate easy assembly. Some significant modifications have 

been made to an earlter spinner design. These improvements gtve 

better efficiency and concentricity of the spinner. Applications are 

illustrated with carbon-13 CP/MAS spectra carried out at different 

rotor spinning rates.

MF21 

SOLID-STATE 13C AND 15N NMR STUDIES OF CROSSLINKING IN 

BACTERIAL CELL WALLS 

Joel R. Garbow* 

Life Sciences NMR Center 

Monsanto Company 

St. Louis, 140 63198. 

Jacob Schaefer 


Washington University 

St. Louis, 140 63130. 

The cell walls of many Gram-positive bacteria are composed of glycan 

backbones with attached short peptide stems. Crosslinks can form 

between amino acids on adjacent peptide stems, contributing to the 

structural integrity of the cell wall; We are using cross-polarization 

magic-angle spinning 13C and 15N NMR to measure the extent and mobility 

of peptidoglycan crosslinks in the cell wall of the bacterium Aerococcus 

viridans. In lyophillzed samples, we use double cross-polarization 

NMR,a technique which detects quantitatively 13C-15N chemical bonds, 

to observe directly the crosslink. Motions of the protein backbone 

and of the crosslink site in both lyophilized and wet-cell samples 

are measured through measurements of NH dipolar and 15N chemical-shift 

tensors. 

The partial collapse of dipolar and chemical-shift tensors for peptide 

NH and for the amide NH at cell-wall crossllnk sites, of intact lyophi- 

lized A. vlrldans cells, indicate NH-vector root-mean-square angular 

fluctuations of 23 °. This result is consistent with the local mobility 

calculated in typical psec-regime computer simulations of protein 

dynamics in the solid state. The experimental root-mean-square angular 

fluctuations for both types of NH vectors increase to 37 ° for viable 

wet cells at I0 ° C. The similarity in mobilities for both general 

protein and cell-wall peptidoglycan suggests that the additional motion 

in wet cells does not involve independent local motions of individual 

cell components.


NMR INVESTIGATIONS OF ATOMIC MICROSTRUCTURE 

IN AMORPHOUS SEMICONDUCTORS 

Q 

Karen K. Gleason , Mark A. Petrich, and Jeffrey A. Reimer, 

.Department of Chemical Engineering, University of California, 

Berkeley, CA 94720-9989. 

The microstructure of amorphous semiconductors has important 

implications for their electronic properties. Nuclear magnetic 

resonance (NMR) can examine the microstructure of these materials 

on an atomic scale. Previous NMR results have indicated that the 

hydrogen in these materials exists both as isolated hydrogen atoms 

and as clusters of hydrogen. Using Multiple Quantum NMR, a 

technique which is able to "count" the number of hydrogen atoms in a 

cluster, we have studied the effects of deposition temperature, 

dopant atoms, and annealing on the clustering of hydrogen in 

amorphous silicon. Our results indicate that electronic device 

quality amorphous silicon films contain small clusters of 

approximately six hydrogen atoms, while nondevice quality films 

contain larger hydrogen atom clusters. We have also extended the 

multiple quantum NMR technique to study a series of amorphous 

silicon carbide alloys, systematically varied in carbon content. We 

have found that small amounts of carbon decrease the total hydrogen 

content of the alloy, but increase hydrogen clustering. Carbon-13 

and silicon-29 magic-angle spinning NMR spectra, taken with and 

without proton decoupling, allow us to probe local bonding 

configurations. These studies have shown that both sp 2 and sp 3 

carbon bonding environments are important in these materials. It is 

especially interesting that nearly all the hydrogenated carbon are 

in the sp 3 bonding configuration. 

By comparing our NMR results with data from other analytical 

techniques such as infrared and optical absorption spectroscopy, 

Rutherford backscattering, and conductivity measurements, we hope 

to elucidate the relationships between deposition chemistry, atomic 

microstructure, and optoelectronic properties of this 

technologically important class of materials. 

Supported by NSF grant DMR-8304163.

MF23 

CESIUM-133 SOLID STATE NMR OF ALKALIDES AND ELECTRIDES 

Lauren E. Hill," Steven B. Dawes and James L. Dye, Department of 

Chemistry, Michigan State University, East Lansing, HI 48824 

Alkalldes and electrldes are crystalline salts In which metal 

cations are complexed with cyclic polyethers or polyamines and the 

resultant anions are either alkali metal anions or trapped electrons. 

Solid state NMR spectroscopy has been extremely useful as a means of 

Identlfying a particular compound and as a probe of the types of 

interactions between an ion and its environment. For example, NMR 

data in combination with structural data on Cs (18C6)2.e" may be used 

to better understand the nature of the trapped electron. The 

temperature dependence gives the contact density of the cesium 

nucleus. A s~udy of the mixed alkalide-electride salt 

Cs (18C6)^.Na e. revealed spectra which consisted of five lines, two 

of which are ~ue To Cs (.8C6) 2 In the pure sodide (-61 ppm) and in the 

pure electrlde (+73 ppm). The other three peaks are evenly spaced 

between th~ electrlde peak a~d sodlde posltions. Since the structures 

of both Cs (18C6)~-e and Cs (18C6)2.Na are known, a superlattice 

which includes ~raered substitution of sodium anions into anionic 

sites in the Cs (18C6)p.e- lattice has been postulated$ Another 

example of the utility-of NMR methods is the ceside CS C222.Cs- in 

which the NMR spectrum consists of two peaks_whlch have been assigned 

to an inclusive and exclusive cation. No Cs peak has been observed. 

The system probably contains a mixture of crystallltes, one type 

having inclusive complexed cations, the other exclusive complexed 

cations. The absence of a Cs signal can be rationalized from the 

structure of thls ceside. These are some examples of how NMR 

spectroscopy in conjunction with x-ray crystallography can be used to 

investigate the nature of these compounds.

MF27 

MULTINUCLEAR SOLID-STATE NMR STUDIES OF DERIVATIZED SILICA GELS 

Robert Zeigler, Greg Quinting, Charle~ E. Bronnimann 

and Gary E. Maciel 



Ft. Collins, CO 80523 

Solid-state NMR has been demonstrated to be an extremely powerful 

technique for probing the structure and dynamics of molecules bound to a 

solid surface (1,2). IH, 15N, 29Si and 13C CP/MAS spectra will be pre- 

sented for silica gels derivatized with APTS (aminopropyltriethoxysi- 

lane). 13C, 15N, IH (CRAMPS) spectra provide evidence regarding the 

nature of the interaction between the amine group of APTS-derivatized 

silica gels and the silica gel surface. 

13C and 29Si NMR techniques have been used to explore the conforma- 

tions and dynamics of dimethyloctadecylchlorosilane(C18)-modified silica 

gel. The effects of both C18 surface concentration and the presence of 

solvents on the C18 chain dynamics have been explored using TCH and 

dipolar dephasing experiments. 

IH CRAMPS, 29Si and 13C NMR are being used to study the nature 

of the silica surface and silica silylation. Several different species 

of protons have been observed on the silica surface and a variety of 

instrumental and chemical techniques are being used to characterize the 

silica surface. 

References 

1. Solid State NMR Studies of Aminopropyltriethoxysilane Modified Silica; 

G.S. Caravajal, D.E. Leyden, G.E. Maciel, p. 283 in Silanes, Surfaces, 

and Interfaces Symposium, D.E. Leyden (ed.) Gordon and Breach Science 

Publ. (1986). 

2. NMR Studies of cl~-Derivatized Silica Systems; G.E. Maciel, R.C. 

Zeigler, R.K. TaTt, p. 413 in Silanes, Surfaces, and Interfaces 

Symposium, D.E. Leyden (ed.) Gordon and Breach Science Publ. (1986).

MF29 

MAGIC ANGLE SPINNING OF MATRIX ISOLATED REACTIVE INTERMEDIATES 

Kurt W. Zilm, Ronald A. Merrill , Marc M. Greenburg, and Jerome A. Berson 

Department of Chemistry, Yale University, P.O. Box 66~6 

New Haven, Corm 06511 

Isolation in inert gas matrices or rigid glasses is widely 

"recognized as an invaluable tool for direct spectroscopic investigation 

of reactive intermediates. CP/MAS NMR has proven to be a most powerful 

technique for studying the structure of amorphous and polycrysta~llne 

solids. However, until now combining MAS technology with matrix 

isolation techniques for the study of ground state slnglet reactive 

intermediates by NMR has proven to be problematic. 

We have developed a CP/MAS probe deslgn which allows rapid transfer 

and subsequent magic angle spinning of sealed 5 mm NMR tubes while 

maintaining the samples temperature at 77 K. The MAS turbine design is 

similar to that reported by Gay in 1984, except that the sample tube 

extends 3 cm below the turbine. The maximum spinning rate obtained with 

our current implementation of this design is 3 kHz. The spinning is very 

stable and remarkably forgiving of imbalances in the tube, both at the 

sample end and at the seal. The unique aspect of this probe design is 

the use of separate gas supplies for cooling and spinning the sample. 

Unlike previous low temperature MAS designs, this MAS probe allows rapid 

transfer of samples prepared outside the probe into the precooled probe 

without warming the sample or exposing it to the atmosphere. With a 

probe of this design one can employ typical photochemical or pyrolytic 

gas phase deposition techniques for preparing intermediates. Virtually 

any ground state slnglet species which can be prepared and is long lived 

at 77 K, can now be investigated by CP/MAS NMR. 

Using this probe design we have observed the first C-13 CP/HAS NHR 

spectrum of a matrix isolated reactive intermediate. The species is the 

singlet biradical 3,4-dlmethylenefuran which gives a single resonance at 

100ppm relative to TMS for the methylene carbons. The biradical, which 

is deep purple, was prepared by photolysis of the corresponding C-13 

labeled(98% at both methylene carbons) azo precursor at 77 K in a 2-MTHF 

glass. After photolysis the decrease in the intensity of the precursor 

peak at 58ppm agrees well with intensity of the new resonance at 100ppm. 

Conclusive assignment of this llne to the biradical can be made on the 

basis of this observation, photobleachlng, and chemical trapping 

experiments. The presence of the NMIR signal demonstrates directly and 

unambiguously the singlet nature of the biradical. Applications to other 

reactive species will also be presented.

MF31 

SECOND OBSERVATION OF IH MASS NMR OF LIPIDS AND MEMBRANES; 

AND 170 CROSS POLARIZATION OF INORGANIC SOLIDS 

by 

Eric O1dfleld,* John Bowers, Jeff Forbes ,. Cynthla Husted, 

Thomas H. Walter and Xi Shan 

University of llllnois at Urbana-Champalgn, 505 South Mathews Avenue, 

Urbana, Illlnols 61801, USA 

We have obtained very high resolution solid-state IH MASS NMR 

spectra of unsonicated liquid crystalline lipid bilayers, and selected 

biological membranes (e.g. rod outer sesments). Resolution is as good 

as with sonlcated, single bllayer vesicles. T1s , linewidths, order 

parameters and 2D experiments wlll be presented. A typical 2D (NOESY) 

experiment on DMPC(I, 2-dimyrlstoyl-sn-glycero-B-phosphocholine) is shown 

below, on the left: 

• • 4' "q 

"'° ~ ° 

]p, ,. ~,o 

~:',. • 

| 4 | | 1 

PPM FROM TM$ 

Drug binding and other studies, will also be outlined. 

--I 

~mzo 

We have also investigated 170 cross polarization in a variety of 

inorganic solids. The type of resolution of overlapping second-order 

quadrupolar broadened powder patterns achievable in complex inorganic 

solids is illustrated by the static and CP results on talc shown above, 

on the right. 

-an 

m


INCREASED RESOLUTION FOR PROTON NMR SPECTRA OF SOLID MATERIALS 

Thomas G. Neiss and James E. Roberts 

Department of Chemistry #6 



Sophisticated multiple-pulse techniques must be used to 

obtain "high resolution" proton spectra of most solid 

materials, or a single broad peak is observed as a consequence 

of the large homonuclear couplings of the proton reservoir. 

When Magic Angle Sample Spinning (MASS) is included with the 

multiple-pulse experiment, the typical proton peak width is 

still between 1 and 2 ppm. When several isotropic chemical 

shifts are present, the resulting spectrum is often not 

interpretable due to significant spectral overlap. Two more 

complicated experiments are available for increasing the 

resolution obtained in proton NMR spectra of solid materials. 

Two-dimensional heteronuclear chemical shift correlation 

NMR has been applied to liquids to connect the proton and 

carbon chemical shifts through J couplings. The J couplings 

in solids are usually not resolved. However, with appropriate 

implementation during MASS, the 2-D experiment correlates the 

proton and carbon chemical shifts, yielding better overall 

resolution in the proton dimension, even though the proton 

linewidths are still 1 to 2 ppm. 

An alternative to the full two dimensional technique 

utilizes selective coherence transfer to observe only specific 

spin systems in a one-dimensional experiment. The selective 

coherence transfer occurs through the strong heteronuclear 

dipolar interaction between bonded spins, so some protons are 

not readily observed with this technique. The gain in proton 

spectrum resolution is comparable to that obtained with 

two-dimensional chemical shift correlation, but data 

accumulation and processing takes less time. Although several 

1-D selective experiments might be needed to fully 

characterize a molecule, it is still a viable approach in many 

situations. 

Acknowledgement is made to the donors of the Petroleum 

Research Fund for partial support of this work. Supported by 

NSF-Solid State Chemistry program grant # DMR-8553275. 

Additional support through the Presidential Young Investigator 

program was obtained from Cambridge Isotope Laboratories; Dory 

Scientific; General Electric Corporate Research and 

Development; General Electric NMR Instruments; IBM 

Instruments; Merck, Sharp and Dohme; and Monsanto Company.

MF35 

RELAXATION MECHANISMS AND EFFECTS OF MOTION IN NaAISi30 s 

LIQUID AND GLASS: A HIGH TEMPERATURE NMR STUDY. 

S.-B. Liu, A. Pines (Dept. of Chemistry, University of California, 

Berkeley, CA 94720) 

*J. F. Stebbins (Dept. of Geology, Stanford University, Stanford, CA 94305) 

The dynamics of atomic or "molecular" motion in molten silicates are poorly known 

"but are of central importance in the understanding of both the thermodynamic and tran- 

sport properties of these complex materials. Despite severe technical problems, l~%,I~R 

spectroscopy on the liquids themselves is potentially a very powerful and perhaps unique 

tool for studying these dynamics. NMR lineshape mad relaxation time studies of 23Na 

and ~Si at temperatures as high as 1200°C have begun to reveal the details of this mo- 

tion, and in particular the local dynamical cause of the macroscopic glass transition. 

For NaA1Si30 s (corresponding to the mineral albite), all 23Na T 1 data from 600 to 

1200°C are above the minimum, indicating the relative high mobility of this "network 

modifying" cation. The dominant spin-lattice relaxation mechanism is found to be qua- 

drupolar interaction which arises from the sodium ion diffusion. The activation energy is 

71-1-3 k J/tool, in close agreement with the results of electrical conductivity and Na tracer 

diffusion data. The correlation time of the Na motion is estimated to be about 8.5x10-11s 

at 1100°C. Relatively minor anomalies in T 1 and T 2 for 23Na are seen at the bulk glass 

transition temperature, indicating that above T s, some Na motion is correlated with 

structural motion of the silicate framework. 

In contrast, all T 1 data for 2gSi in the same temperature range are below the 

minimum, because of the relative immobility of this "network former". Most 

significantly, dramatic changes in the ~Si T 1 slope, and in the relaxation mechanism, 

occur at the bulk glass transition temperature, indicating a rather abrupt increase in the 

extent of structural motion at the same point where abrupt changes in thermodynamic 

properties occur. Both dipole-dipole interactions and the chemical shift anisotropy 

known from crystals and glasses contribute to the 2QSi spin-lattice relaxation above the 

glass transition, but are insufficient to completely account for the observed T 1 values. 

Relaxation may therefore involve short lived distortions of the structure which cause 

temporary excursions in chemical shift several times greater than those which can be 

quenched into the glass.

MF37 

A Unique Method for the Quantitative Determination of Mixed Liquid 

and Solid Phases Using Solid-State NMR Techniques 

Evan H. Williams 

Varian Associates, 611 Hansen Way, Palo Alto, California 94303 

Many apparently solid materials axe, in fact, mixtures of both solid and liquid 

phase components. It is not easy to investigate the morphology of such systems, 

particularly in a non-invasivc way. NMR provides such a means for both solid and 

liquid phases, but suffers from a lack of a readily acccssiblc, absolute quantitation. 

An NMR technique has been developed that overcomes this problem, allowing 

simultaneous observation of both phases in a manner that allows quantitation. Among 

other possibilities, use of spectral editing allows the separation of the two phases into 

separate subspectra. Such subspectra allow the observation of adsorption in the 

presence of excess material in a quantitative way. Another use of the technique has 

been found in the investigation of the kinetics of curing of network polymers 1. 

A detailed description of the methodology and its application to a number of 

representative systems will be presented. 

1p.E.M. Allen, etal, Eur. Polym. J., 22. 549, (1986).

MF39 

HIGH RESOLUTION DNP-NMR AND KNIGHT SHIFt SUPPRESSION IN A 

ONE DIMENSIONAL CHARGE TRANSFER CONDUCTOR 

R. D. Kendrick, H. Seidel? a, D. A. Singel, TM 

W. StOcklein, lc* and C. S. Yannoni 

IBM Almaden Research Center, San Jose, CA 

Over the last few years, a wide variety of magnetic resonance experiments have been 

performed on a new class of charge transfer complexes which exhibit high one-dimensional 

conductivity (~100 (~2 cm)'l). 2 Since the linewidth of the ESR due to the conducting spins 

is extremely narrow (~10 milligauss at 9 GHz), proton Overhauser enhancements as high 

as 525 have been achieved in this material. 2a 

We report here a 13C NMR study of the fluoranthenyl (FA) radical cation salt (FA):PF 6. 

Using a 60 MHz DNP spectrometer based on a Fabry-.Perot cavity? we have been able to 

observe signals from as few as 1016 carbon-13 nuclei in a single scan at room temperature. 

The Knight shift of the 13C spins 2c depends on the difference in population between 

electron Zeeman levels: thus, by saturating the ESR line, we have been able to suppress the 

Knight shift. A study of the power dependence of this suppression permits correlation of 

the Knight and chemical shifts. 

The ramifications of a variety of other interactions such as the shift of the ESR line due 

to saturation with microwaves (Overhauser shift 2a) or to the proton and fluorine 

decoupling fields (Bloch-Siegert shift) will be discussed. 

_ --'4- 

m -- 2 

(FA) 2PF 6 

PF 6" 

1. Current address: (a) Physics Department, Stuttgart University; b) Chemistry 

Department, Harvard University; (c) Physics Department, Bayreuth University. 

2. (a) W. St0cklein and G. Derminger, Mol. Cryst. Liq. Cryst. 136, 335 (1986) and 

references therein; (b) H. Brunner, K. H. Hausser, H. J. Keller and D. Schweitzer, 

Solid State Comm. 51,107 (1984); (c) M. Mehring, M. Helmle, D. KOngeter, G. G. 

Maresch and S. Demuth, Proc. of the Intl. Conf. on Synthetic Metals, ICSM86, Kyoto, 

Japan, 1986 (to be published in Synthetic Metals). 

3. R.D. Kendrick, H. Seidel, D. A. Singel and C. S. Yannoni (to be published).

MF41 

ACETYLCHOLINE RECEPTOR --AGONIST BINDING. 

RESULTS FROM SELECTIVE RELAXATION NMR EXPERIMENTS. 

Ronald W. Behling °, Tetsuo Yarnane, Gil Navon t, 

Michael J. Samrnon, and Lynn W. Jelinski 

AT~T Bell Laboratories Murray Hill, New Jersey 07974 

t Tel-Aviv University, Israel 

Selective proton NMR relaxation mea-~urements were used with nicotine 

titrations to obtain relative binding constants for nicotine, acetylcholine, 

muscarine, and carbamylcholine binding to purified acetylcholine receptors from 

Torpedo californica. The results show (1) that the binding constants are in the 

order acetylcholine > nicotine > carbamyl choline > muscarine; (2) that 

selective and non-selective NMR measurements provide a rapid and direct 

method for monitoring both the specific and non-specific binding of agonists to 

these receptors; (3) that a-bungarotoxin can be used to distinguish between 

specific and non-specific binding to the receptor; (4) that the receptor-substrate 

interaction produces a large change in the selective relaxation time of the 

agonists even at concentrations 100x greater than that of the receptor. This 

latter observation means that these measurements provide a rapid way to 

measure drug binding when only small amounts of receptor are available, and 

that they may be useful for determining the conformation of the small ligand in 

its bound state.

MF43 

DESIGN AND USE OF A PULSE SHAPER FOR HIGH RESOLUTION NMR. 

Kermit M. Johnson* and Klaas Hallenga 

Michigan State University, Department of Chemistry 

East Lansing, MI 48824 

Although the use of tailored excitation in high resolution NMR has 

been suggested on several occasions, the method has been used only 

sporadically due to the poor performance of existing circuitry. 

The solution of the Bloch equations for perfect frequency 

selective inversion by Hoult et al (I) and the possibility of computer 

designed highly selective excitation makes it desirable to have pulse 

shaping capability routinely available. 

We have implemented a flexible pulse shaping circuit on our 

spectrometer (Bruker WM-250 with Aspect 2000) which will deliver 

amplitude and phase modulated pulses. The device uses two IK x 12 bit 

buffers feeding two identical 12 bit D/A converters. The rate at 

which the waveform is read out of the buffers is controlled by a 

variable frequency clock. 

The outputs of the DAC's control separately the amplitudes of 

quadrature radio-frequency signals which are recombined to form a 

shaped pulse which may thus vary in both amplitude and phase. 

Additionally, this circuit could be easily modified to perform phase 

shifting of the rf pulse after the method of Sears (2). The device is 

easily loadable under computer control with any desired waveform. 

Finally, no spectrometer hardware or software modifications were 

required to use the pulse shaper. 

Details of the circuitry, test results, and some applications to 

ID and 2D NMR experiments will be demonstrated. 

(I) M. S. Silver, R. I. Joseph and D. I. Hoult, J. Magn. Res. 59, 347 

(198~). 

(2) R. E. J. Sears, Rev. Sci. Instrum. 55, 1716 (1984). 

a

MF45 

THE USE OF D=O AS A MOLECULAR PROBE 

IN DETERMINING DNA SOLID STATE PACKING 

Rolf Brandes,* David R. Kearns, and Allan Rupprecht7 

Department of Chemistry, University of California-San Diego, 

La JoUa, CA 92093, rArrhenius Laboratory of Physical 

Chemistry, University of Stockholm, Stockholm, Sweden 

We have used high resolution =H NMR of DzO to monitor the packing of 

hydrated DNA molecules in solids prepared from solution by three different 

methods: lyophilization, alow evaporation of the water, and wetspinning in alcohol 

which produces uniaxially oriented DNA. The two latter methods resulted in thin 

films of DNA, which were also broken up to obtain macroscopically isotropic sam- 

pies. These five samples all showed different spectral shapes with different spin- 

spin relaxation times Tz,. 

With lyophilized DNA, the spectral shape can most reasonably be interpreted 

in terms of isotropic packing. The evaporation method produces spectra which are 

consistent with a spontaneous cholesteric ordering of the DNA. The order is 

macroscopic, with the pitch axis perpendicular to the plane onto which the DNA 

dried. Even when macroscopic order is not obtained, spin-spin relaxation experi- 

ments can be used to determine if the sample consists of local domains with 

cholesteric or uniaxial ordering of DNA molecules. For the case of the uniaxially 

oriented DNA prepared by wetspinning, a 2-dimensional technique is used to 

separate the contributions to the linewidth arising from DNA static disorder, mag- 

netic inJaomogeneities, and spin-spin relaxation. This separation enables an upper 

estimate of the fiber disorder if a Gaussian distribution of the helix axes is 

assumed with a standard deviation of ,,-12 " ^ 

IBD-NMR spectrum of uniazially oriented DNA.

MF47 

SOLID STATE NMR STUDIES OF ISOTOPICALLY LABELED GAMICIDIN A 

IN AN ORIENTED LIPID BILAYER 

L.K. Nicholson*, F. Moll III, P.V. Ix)Grasso, C.A. Guy, T.A. Cross 


and 

Institute of Molecular Biophysics 

Florida State University, Tallahassee, FI. 32306-3006 

2H and ISN isotopic labels have been incorporated into the linear 

polypeptide, Gramicidin A by a variety of techniques including bio- 

synthesis, chemical peptide synthesis and exchange. The labeled 

Gramicidins have been incorporated into lipid bilayers where a dimer 

of the polypeptide forms a monovalent cation selective channel across the 

synthetic membrane. Some of the samples have been oriented such that 

the channel axis is parallel with the magnetic field. The samples have 

been characterized by circular dichroism, differential scanning 

calorimetry and NMR. 

Solid state NMR experiments are being used to elucidate an atomic 

resolution image of both the dynamics and structure of the channel. 

Interpretation of the high resolution spectra of oriented samples has 

provided bond orientations with respect to the channel axis. Analysis 

of powder patterns has provided data for the large amplitude motions 

of the polypeptide backbone.

MF49 

Solid State 2H NMR Studies of Biphenyl in the l~-Cyclodextrin Clathrate Complex 

Alan D. Ronemus*, Robert L. Void and Regitze R. Void 

Depamnent of Chemistry B-O14, University of California at San Diego, La JoUa, CA 92093 

Cyclodexu'ins are cyclic oligosaccharides comprised of D-glucose units connected by alpha-l,4- 

glycoside linkages, forming a hydrophobic cavity which readily binds a variety of guest molecules to 

make inclusion eomplexesJ The nature of guest motion in such complexes is of interest because 

cyclodextrins have been utilized as enzyme models and as stabilizing agents for pharmaceuticals, 

pesticides, flavors, and essences. Biphenyl should form a channel clathrate with I]-cyclodextrin, which is 

of particular interest as the guest motion may resemble processes in the core region of thermotropic 

liquid crystals. Previous studies of the dynamics of guests in cyclodextrin clathrates in solution have used 

EPR spin probes, 2 and high resolution l~'oton and lSC NMR? '4 while in the solid state lSC CP-MAS 5 and 

static 2I-I NMR 6 have been employed. 

Solid state static 2H NMR is particularly well suited to the study of motional dynamics as powder 

lineshapes are sensitive to motional processes with rates in the range of 103-107 s "-1. Further, the 

quadrupolar interaction dominates to the extent that other interactions generally may be neglected, while 

being small enough as to be experimentally and theoretically tractable. 

In order to obtain undistorted lineshapes it is necessary to use the quadrupolar echo sequence. 7 A 

program has been developed to simulate spectra from quadrupolar echoes, including the effects of 

exchange during the delays and prises for several independent motional processes and finite pulse length, 

allowing the determination of motional parameters for appropriate models, s 

Solid state 2I-I NMR powder spectra of 4,4"-d2-biphenyl and biphenyl-dl0 in ~-cyclodexlrin have 

been obtained over the temperature range from 103 to 303 K at several echo delay times. The lineshape 

is strongly dependent on temperature over the range measured, approaching the fast motion limit at 303 

K and the rigid limit at 103 K. The stx~tra may be interpreted in terms of two independent motional 

processes: libration of the long axis of the molecule over a restricted range of angles, and hopping of the 

rings in the four well internal torsional potential with two different barrier heights. 9 Rotation about the 

long axis appears to be severely hindered as it occurs at rates no greater than 100 s -~ at 303 K. The 

libration was modeled as all-site jumps on uniform geodesics with various grid spacings to approximate 

motion in a cone of half-angle 27.5 degrees. It was found that a minimum of nineteen sites was required 

to reproduce the experimental lineshapes for the para-deuterated complex, with rates ranging from 1 × 

103 s -~ at 103 K to 4 x 106 s -~ at 303 K. The internal hop was modeled as a four site nearest neighbor 

jumping process with different rates to each neighbor. The inter-ring torsion angle of 39 degrees agrees 

with the angle determined in the vapor phase 1° and in solution? l and with theoretical calculations? At 

303 K the fast rate was 4 x 107 s -1 while the slow rate was 4 x l0 s s -l. Further simulations are in 

progress to define the motional parameters across the entire range of temperatures studied. Single-crystal 

rotation spectra of biphenyl-d~0~-cyclodextrin have been produced which indicate that the structure is of 

the "screw-channel" type. 

1. J. Szejtli, "Cyclodextrins and Their Inclusion Complexes," Akademiai Kaido, Budapest, 1982. 

2. K. Flohr, R. M. Patton and E. T. Kaiser, J. Am. Chem. Soc. 97, 1209 (1975). 

3. J. P. Behr and J. M. Lehn, J. Am. Chem. Soc. 98, 1743 (1976). 

4. R. J. Bergeron and M. A. Channing, J. Am. Chem. Soc. 101, 2511 (1979). 

5. H. Ueda and T. Nagai, Chem. Pharm. Bull. 29, 2710 (1981). 

6. L. D. Hall and T. K. Lira, J. Am. Chem. Soc. 106, 1858 (1984). 

7. J. H. Davis, K. R. Jeffrey, M. Bloom, M. I. Valic and T. P. Higgs, Chem. Phys. Len. 42, 390 (1976). 

8. M. Greenfield, A. Ronemus, R. L. Void, R. R. Void, P. Ellis and T. Raidy, J. Magn. Reson., 70 (1986). 

9. G. Haefelinger and C Regelmann, J. Comput. Chem. 6, 368 (1985). 

10. O. Bastiansen and S. Samdal, J. Mol. Struct. 128, 115 (1985). 

11. M. Barret and D. Steele, J. Mol. Struct. 11, 105 (1972).

! 

1.7 

MF51 

ULTRA-HIGH RESOLUTION IN IH SPECTRA AT $00 MHZ: 

CHLORINE ISOTOPE EFFECTS 

Frank A. L. Anet and Max Kopelevich* 

Department of Chemistry and Biochemistry 

University of California, Los Angeles 

Los Angeles, CA 90024 

We have observed chlorine isotope effects on the IH nuclear shielding in chloroform 

and methylene chloride. These effects are on the order of 0.2 ppb and are readily detectable 

at high fields (11.4"13 provided some care is taken in sample preparation and in optimizing 

field homogenuity. Application of Lorentzian-Gaussian resolution enhancement allows 

baseline separation of the resonance lines with areas corresponding to statistical weights of 

the various C135/C137 isotopic combinations, as shown below. This appears to be the first 

example of chlorine isotope effects on IH shifts. 

We are currently undertaking studies of isotope effects in other halogenated 

methanes, exploring the solvent dependence of these effects, as well as looking into different 

means of obtaining ultra-high resolution spectra. 

' '5 ' ' ' ' '0 ' , , i 

HERTZ 

500 MHz IH{D} spectrum of 2% CHDCI 2 in CD2CI 2. Ratios of the areas are approximately 

9:6:1.


DI-13C-LABELING: A MEANS TO MEASURE 12C-13C 

ISOTOPIC EQUILIBRIA IN 2-NORBORNYL CATION. 

Ronald M. Jarret*, Department of Chemistry, College of the 

Holy Cross, Worcester, MA 01610. 

Martin Saunders, Department of Chemistry, Yale University, 

New Haven, CT 06511. 

2,3-Di-13C-norborn-2-yl chloride was prepared and 

ionized (with SbF 5) to 2-norbornyl cation. In solution 

at -65°C, rapid rearrangements occur which completely 

scramble the 13C-labels. The proton-decoupled cmr 

spectrum (62.7 MHz) contains three signals: C-4, C-I,2,6 

(averaged), and C-3,5,7 (averaged). The 13C-labels are 

thus equilibrated over non-equivalent sites within 

2-norbornyl cation. This 12C-13C equilibrium isotope 

effect alters the proportion of di-13C-labeled isomers 

from statistical values. The non-statistical isotopic 

isomer population is manifested as an asymmetric 

multiplet for the averaged C-3,5,7 peak in the cmr 

spectrum. The relatively sharp lines of the multiplet 

can be reproduced within ± 0.i ppm, with isotopic 

equilibrium constants of K-3,5,7 = 1.010 t 0.005 and 

K-I,2,6 = 1.039 t 0.005. 

71 

6 

4 8 

CI(H) 

H(CI)

MF55 

DYNAMIC PARAMETERS FROM NONSELECTIVELY GENERATED ID EXCHANGE SPECTRA 

Charles G. Wade, Mark O'Neil-Johnson, and Eric R. Johnston 

IBM Instruments, Inc. 

40 Airport Parkway 

San Jose, California 95110 

We propose an experimentally and computationally simple method 

for the direct measurement of the elements of the relaxation matrix 

R which characterize dynamics in spin systems. The usual 2D exchange 

pulse sequence (90 ° ) - t I - (90 ° ) - t m - (90o ) - t2(obs) is used, 

with appropriate phase cycling for the cancellation of single quantum 

and higher-order coherence during t m. For a system of N spins we 

record spectra with and without mixing for N arbitrarily chosen values 

of t I. This affords N 2 measureable intensities from which the N 2 

elements of e -~tm can be generated and from which R itself can then 

be calculated with a back-transformation method. 

The utility of the method lies in the ease and speed with which 

the experimental data are generated. Only nonselective transmitter 

pulses are required so the method is easier to implement than other 

schemes which employ DANTE or decoupler inversion pulses to perturb 

the spin system prior to mixing. Time-consuming 2D data acquisition 

and processing are similarly avoided. The method will be illustrated 

with applications to multisite and scalar-coupled spin systems.

MF57 

CALIBRATED DECOUPLING OF TIGHTLY-COUPLED CONCENTRIC SURFACE 

COILS FOR IN VIVO NMR 

M. Robin Bendall 

Experimental work carried out at Varian Fremont Operations, CA, 

whilst on leave from Griffith University, Nathan, Qld., Australia 

A considerable research effort has been expended on localization 

methods for in vivo spectroscopy that depend on using rf coils 

such as surface coils which provide inhomogeneous rf fields. The 

most complete means of signal localization utilize rf pulses (eg 

depth pulses) from two coils and this general technique requires 

an active method for detuning each coil during the rf pulses 

from the other coil. 

Recently we described the successful implementation of an active 

detuning scheme which depends on the use of I/4 cables to block 

rf current in a coil (I). Here we will provide further experi- 

mental details of this method and compare it experimentally to 

three other methods of active detuning. 

A new finding of particular importance is the discovery that not 

only can we completely detune a transmitter coil so that it has 

no effect on the rf field of a neighbouring coil, but by offsett- 

ing the detuning of the coil, a calibrated fraction of the rf 

field of the detuned coil can be added to or subtracted from the 

rf field of the neighbouring coil. This principle is general and 

should be applicable to any active detuning method which relies 

on the introduction of a second circuit resonance at the frequen- 

cy of interest, as for the four schemes tested. This principle 

allows the shape of the rf field of one coil to be modified in a 

calibrated fashion by the second coil. The use of two transmitter 

coils for signal localization depends on the two coils having 

markedly different rf fields, and this difference can obviously 

be increased by subtraction of a fraction of the rf field of one 

coil from the second. Experimental details of this general method 

for controlling the shape of the two inhomogeneous fields 

provided by two tightly-coupled rf coils will also be given. 

(1) M.R. Bendall, D. Foxall, B.G. Nichols and J.R. Schmidt, 

J. Magn. Reson. 7__0,181 (1986).

MF59 

THE CONE COIL - AN RF GRADIENT COIL FOR SPATIAL ENCODING ALONG 

THE B 0 AXIS IN ROTATING FRAME IMAGING EXPERIMENTS 

John P. Boehmer and Richard W. Briggs* 

Departments of Radiology and Biological Chemistry 

M. S. Hershey Medical Center, Pennsylvania State University 

Hershey, Pennsylvania 17033 

The rotating frame zeugmatography experiment (1) is a useful alternative 

to NMR imaging using static field gradients, especially for chemical 

shift imaging or for species with short transverse relaxation times. 

However, application of the method and its modifications (2-4) has been 

limited to one-dimensional imaging. Hoult has proposed a way to achieve 

2D imaging by combining RF and static field gradients (1). His group has 

reported an algorithm for rapid reconstruction of a 2D rotating frame 

image (5), and Haase has described an orthogonal coil system by which 2D 

rotating frame imaging (RFI) can be done (6). The first 2D rotating 

frame image was shown a year ago (7). 

Both ID and 2D RFI methods have been able to localize NMR signals 

only in spatial directions perpendicular to the static field B o. This is 

because RF coils designed to date create gradients in RF intensity 

parallel to the flux lines of the B 1 field, and spin nutation is effected 

only for orthogonal components of B o and B I flux lines. 

An RF coil in which the gradient in RF field intensity is orthogonal 

to the flux lines of B 1 would permit RFI to be done along the B o field 

direction, and make possible full 3D imaging with RF gradients alone. 

One design which achieves the desired orthogonality of the B 1 

gradient and B 1 flux lines is a Helmholtz coil tapered such that the 

diameter at one end is greater than the diameter at the opposite end. 

Sample at the smaller end thus experiences a greater RF field intensity 

than at the larger end. Birdcage coils modified analogously also produce 

the desired orthogonality. These cone-shaped coils make full 3D RFI 

feasible, with the attendant rotating frame advantages of retention of 

chemical shift information and effectively instantaneous gradient 

switching. 

I. D.I. Hoult, J. Magn. Reson. 33, 183-197 (1979). 

2. K.R. Metz and R.W. Briggs, J. Ma_~g~_n. Reson. 64, 172-176 (1985). 

3. M. Garwood, T. Schleich, B.~Ross, ~]~]--~a~on, and W.D. Winters, 

J. Magn. Reson. 65, 239-251 (1985). 

4. I~. ~o~-T]-. S~leich, M.R. Bendall, and D.T. Pegg, J__s. Magn. 

Reson. 65, 510-515 (1985). 

5. ~C~n, D.I. Hoult, and V.J. Sank, Magn. Reson. Med. i, 354-360 

(1984). 

6. A. Haase, Poster 72, 3rd Ann. Mtg. of the Society of Magnetic 

Resonance in Medicine, New York, New York, August 13-17, 1984. 

7. J.P. Boehmer, K.R. Metz, and R.W. Briggs, Poster A18, 27th ENC, 

Baltimore, Maryland, April 13-17, 1986.

MF61 

AN IMAGING NETHOD OF SHIMMING FOR SPECTROSCOPY 

Truman R. Brown* • Kark S • Cohen ÷ and William J Thoma 

Fox,Chase Cancer Center. Philadelphia. PA 19111 

Siemens Nedical Systems. Aston. PA 19014 

The acquisition of NMR spectra from human subjects with adequate frequency 

resolution in a NMR imaging magnet requires the magnetic field be 

significantly more homogeneous than during an imaging experiment. In the 

normal solution to this problem, shimming on the signal produced by a surface 

coil• the resultant FID is weighted toward the regions clos~ to the surface 

coil which are often not the regions of interest. It seems sensible to make 

use of the imaging capabilities of the system to determine and shape the field 

distribution in the region of interest. 

This can be accomplished by employing a pulse sequence before a normal 

imaging experiment which ~enera~es an image dependent on the homogeneity of 

the magnetic field. A 90v-r-90 v sequence in place of the initial 90 pulse of 

a normal spin-echo imaging sequence generates an image in which the phase 

variation across the sample due to the magnetic field is cony%ted into 

intensity variations. A 4B ° rf phase shift between the two 90 pulses allows 

the sign of the change in the field to be determined. 

A value of • greater I/vAH where AB is the overall field inhomogeneity 

will result in an image with m~Itipl~ bards of constant intensity 

corresponding to a difference of 360 in phase. A shorter ~ will result in a 

single-valued conversion between intensity and phase which allows the image to 

be directly converted into a field map. 

Thus, it should be possible to adjust the homogeneity of a 1 M bore magnet 

for spectroscopy based on data generated in the imaging mode. The technique 

should also prove useful, particularly after automation, to shim a volume 

selected region when the selection procedures do not allow direct shimming.

MF63 

NON-INVASIVE SPIN LABELING OF BLOOD BY ADIABATIC FAST PASSAGE 

Thomas Dixon ~, Leila N. Du ~, and Mokhtar Gado ~ 

~Emory University, Department of Radiology, Atlanta, 

Georgia 

~Washington University, Department of Physics, St. 

Louis, Missouri 

~Mallinkrodt Institute of Radiology, Washington 

University, St. Louis, Missouri 

Excellent images of arteries can be made usinm X-rays, if 

contrast is provided by injecting iodine compounds through 

catheters into the arteries. Unfortunately, these injections 

make the procedure more time consuming, expensive, painful and 

dangerous than an NMR exam. 

While NMR has long produced excellent images of brains and 

even beating heartS, its use on rapidly flowing blood is in its 

infancy. Our approach has been to modify the pulse sequence to 

resist the problems of motion and to trigger our pulses during a 

phase of the heartbeat when the blood is still. 

Stationary blood can be distinguished from other stationary 

tissues if it has been labeled by spin inversion before the image 

is produced. Our approach is to use an adiabatic fast passage in 

which neither the frequency nor the magnetic field are swept. 

Instead, natural motion of arterial blood in an applied field 

gradient causes the Larmor frequency of the blood to sweep past 

the transmitter frequency. Stationary tissue is thus not 

affected. Images of blood only are produced by subtracting an 

image with fast passage from one without, just as subtraction is 

used in the conventional X-ray images to eliminate interfering 

bone shadows. 

Images of the neck will be presented and 

other problems will be discussed. 

dynamic range and

MF65 

NMR IMAGING WITH EXTREMELY INHOMOGENEOUS B1 FIELDS 

M.Garwood', K. UgurbU, Gray Freshwater Biological Institute, 

UniverMty of Minnesota, Navarre, MN 55392. 

M.R. Bendall, School of Science, Griffth University, 

Nathan Queensland 4111, Australia. 

D.L. Foxall, A.R. Rath, Varian Fremont Operations, 1120 Auburn Rd, 

Fremont, CA 94538. 

A critical requirement in many NMR experiments is the ability to induce 

rotations of the magnetization vectors uniformly over the entire sample. This 

requirement is especially severe in NMH imaging and localized spectroscopy. Con- 

sequently, intense efforts are invested in designing RF coils that generate uniform 

B 1 fields. An alternative approach to eliminating problems related to B 1 inhomo- 

geneities is to generate pulses that are highly insensitive to B 1 variation. Two such 

pulses that create transverse magnetization and carry out spin inversion have been 

described [1,2]. These pulses, however, cannot execute a plane rotation with a well 

defined phase. A pulse that provides a 180 ° plane rotation is needed for experi- 

ments that require refocusing. We have recently introduced amplitude and 

frequency/phase modulated pulses derived from the adiabatic passage principle 

that can achieve 90 ° and 180 ° plane rotations [3,4,5]. When optimized, uniform 

90 ° and 180 ° rotations can be obtained over a 50 to 100 fold variation in B 1 field 

strength with these new pulses. This insensitivity to B 1 permits the execution of 

experiments that require uniform RF fields, such as NMR imaging, with coils that 

generate inhomogeneous fields such as the simple surface coil. We have success- 

fully made NM~ images with these new adiabatic pulses using a surface coil for 

both transmission and reception. The results to be presented include; a series of 

images with slice planes selected either parallel or perpendicular to the plane of the 

coil and the design of the pulse sequence used for this work. 

REFERENCES: 

[1] M.S. Silver, R.I. Joseph & D.I. Hoult (1984) J.Mag.Reson. 59,347. 

[2] M.R. Bendall & D.T. Pegg (1986) J.Mag.Reson. 67,376. 

[3] K. Ugurbil, M. Garwood & M.R. Bendall (1987) J.Mag.Reson (In press). 

[4] M.R. Bendall, M. Garwood, K. Ugurbil & D.T. Pegg (1986) (Submitted). 

{5] K. Ugurbil & M. Garwood (1987) (Submitted).

MF67 

MAGNETIC RESONANCE IMAGING WITH PHASE-MODULATED STORED WAVEFORMS 

Petra Schmalbrock, *,a Annjia T. Hsu, b 

William W. Hunter, Jr. a and Alan G. Marshall, b,c 

Dept. of Radiology, a (Dept. of Chemistry, b Dept. of BiochemistryC), 

The Ohio State University, Magnetic Resonance Imaging Facility, 

1630 Upham Drive, Columbus, OH 43210 

Slice location in magnetic resonance imaging is typically achieved 

by irradiation with narrow-bandwidth rf pulses in combination with 

magnetic field gradients. However, theoretically optimal waveforms 

require a large time-domain dynamic range and can perform poorly 

experimentally--e.g., impreci se slice definition and T 2 errors in 

spin-echo imaging experiments. 

Our recently demonstrated Stored W_aveform Inverse F_ourier T_ransform 

(SWIFT) technique I can generate any desired spectral profile while 

minimizing the dynamic range of its time-domain representation. In this 

poster, we report images in which slice selection was achieved with 

SWIFT-generated waveforms on a GE 1.5 Tesla Signa ® whole-body imaging 

system. Time-domain waveforms were generated by quadratic phase 

modulation of a specified discrete excitation magnitude spectrum. 

followed by inverse discrete Fourier transformation and apodization to 

give a stored time-domain waveform that could then be clocked out via 

real-time digital-to-analog conversion to the rf transmitter. SWIFT 

waveforms for slice selection will be compared to the usual sin(x)/x 

slice-selective pulse and to recent computer simulations by Kunz. 2 

[This work was supported by N.S.F. CHE-8218998, General Electric 

Company, and The Ohio State University.] 

1. Hsu, A. T.; Hunter, W. W.. Jr.; Marshall, A. G.; Schmalbrock, P.; J. 

Magn. Reson. (1987), in press. 

2. Kunz, D.; Magn. Reson. Med._3, 377 (1986).

MF69 

28th ENC Poster Abstract 

DOUBLE QUANTUM FILTERED NMR IMAGING, 

PROGRESS TOWARD METABOLITE SPECIFIC IMAGES 

Paul J. Kellerea, Petra Schmalbrockb,and Charles Dumoulin c 

a) Barrow Neurological Institute, 350 W. Thomas Rd. 

Phoenix, AZ 85013 (602)285-3179 

b) Dept. of Radiolo~, Ohio State University, 1630 Upham Dr. 

Columbus, OH 43210 

c) General Electric Research and Development Center, PO Box 8 

Schenectady, NY 12301 

We are currently exploring proton double quantum 

filtration methods as the basis for production of metabolize 

specific images using a clinical 1.5 Tesla MR imaging system 

equipped with a 1 meter bore solenoid. Lactic acid is an 

attractive target metabolite since it is formed in high 

concentration in ischemic tissues and its 1H-NMR pattern 

approaches a first order A3X system at 1.5 T. Double quantum 

filtration is accomplished-by the RF sequence, 90O-TJ-180 o- 

TJ-9OO-TV-90 ° where TJ=I/8J and TV is the double quantum 

evolution time. Double quantum selection is done by both RF 

phase cycling and by pulsed magnetic field gradients. One 

field gradient pulse is given during TV and a second pulse of 

twice She amplitude is given immediately after the last RF 

pulse. ~ This sequence of RF and gradient pulses is followed 

by a slice selective 180 ° pulse and the usual spin-warp phase 

and frequency image encoding. 

The suppression of water, as well as other non-J-coupled 

signals is accomplished by, a) RF phase cycling, b) gradient 

induced dephasing, and c) the temporal separation of the 

coherence transfer echoes arising from double and single 

quantum coherence during TV. Substantial suppression of 

lipid methylene signals is obtained due to the use of 1/8J 

for TJ which leads to inefficient double quantum excitation 

of second order systems. 

Work thus far has been conducted using a phantom 

consisting of three bottles containing water, cooking oil and 

aqueous sodium lactate, respectively. Images showing only 

i M lactate have been obtained using a 128 x 256 image matrix 

and two excitations (8 min. acquisition time). Current 

efforts are aimed at further suppression of unwanted signals 

arising from double quantum coherence and programing to 

permit smaller image matrices. 

1) A.Bax, P.G.de Jong~ A.F.Mehlkopf, J.Smidt, J.Phys.Lett., 

6_2.567 ( 198o ).

MF71 

A DESIGN OF HOMOGENEOUS SELF-SHIELDING GRADIENT COILS 

I. J. Lowe 

Physics Department, University of Pittsburgh, Pittsburgh, PA 

15260 and Department of Biological Sciences, Carnegie Mellon 

University, Pittsburgh, PA 15213 

Magnetic field gradients are of fundamental importance in NMR 

imaging and volume localization techniques. For apparatuses 

with cylindrical symmetry, these gradients are usually 

generated by discrete coils wound on cylindrical formers (of 

radius R). These coils are usually designed using spherical 

harmonic or Taylor expansions of magnetic fields due to 

current distributions (I). The gradients are usually 

satisfactorily linear over a spherical volume of less than 

0.5 R. Further, these gradients are normally time dependent 

and the fringing magnetic fields generate eddy currents in 

the surrounding metal surfaces that can produce undesirable 

magnetic field inhomogeneities and time dependences. 

We have developed a calculational technique based upon 

Maxwell's Equations along with conditions of rotational and 

translational symmetries to find the behavior of the desired 

magnetic field over all of space. From these fields, the 

necessary current density distributions on the surface of a 

cylinder of radius R I are derived for x, y, and z gradients. 

These gradients are perfectly homogeneous inside the cylinder 

for the described current distribution and a long enough 

cylinder. 

It has been suggested (2-5) that a dynamically driven shield 

can be designed to cancel the fringing field outside of a 

second cylinder of radius R 2 (R 2 > RI). We further describe 

the current distribution on the surface of this second 

cylinder that perfectly shields the fringing field of the 

first cylinder. 

I. F. Romeo and D. I. Hoult, Hag. Res. in Med. ~, &4 

(1985). 

2. p. Mansfield and B. Chapman, J. Phys. E. Sci. Instr. 

I__99, 540 (1986). 

3. B. Chapman and P. Mansfield, J. Phys. D. Appl. Phys. I__99, 

L129, (1986). 

4. P. Mansfield and B. Chapman, J. Magn. Reson. 66, 573 

(1986). 

5. R. Turner and R. M. Bowley, J. Phys. E. Sci. Instr. I__99, 

876 (1986).

MF73 

OXYGEN-17 MAGNETIC RESONANCE IMAGING (OMRI) 

G. D. Mateescu and Terri Dular 

Department of Chemistry, Case Western Reserve University 

Cleveland, Ohio 44106 

In spite of the primordial importance of oxygen in llfe processes and in 

many fields of chemistry, imaging with oxygen-17 has not yet been attempted. 

This is due to the fact that O-17 has generally been considered impractical for 

MRI, owing to its "unfavorable" properties: very low natural abundance, low 

natural sensitivity, and considerable quadrupolar broadening. 

We report the first 170 imaging experiments and present evidence that the 

above mentioned "drawbacks" can be turned into advantages. In the absence of 

specialized equipment, our approach was es- 

sentially the same as in Lauterbur's histo- 

rical endeavor. The results shown in Figure 

1 are selfexplanatory . Further experi- 

ments demonstrated the feasibility of OMRI 

with plants, animal blood, brain, kidney, 

heart, muscle, fat, eggs, as well as non- 

biological matter. Contrasts from drastic 

to very subtle can be obtained in TI, T2, 

density, and flow measurements. A dramatic 

"Reverse Gradient Imaging" was obtained 

with signals from water in extreme (bound & 

DOG BLOOD (b) 

Natural a b u n ~ 

lATER 

Natural abundance 

! t I 

i i i 

i i 

• I I 

g~ 

Z-gradient 

0.2 G/cm 

free) states. Combining IH and 170 imaging Figure I. O*yge,-17 Magnetlc Resonance Imaging. 

(a) Two NH,q tubes (5mm OD) containing distilled 

water, placed in a 16mm tube containing CDC1]. 

proves to be useful. 170 is a better repre- (b) Two NMR tubes containing dog blood. 1200 90 ° 

pulses at O.l s intervals per trace. Varian XL- 

200 at 27.12 ~z. We expect a >80 times better 

sentative of the H20 molecule. Its relaxa- resolution with the 20G/cm mlcrolmager co be in- 

stalled In February 1987 on our Bruker MSL-&O0 

tlon depends essentially on intramolecular (local protein, nucleic acid, 

lipid, sugar) electric field gradients; also, 170 relaxation is mainly affected 

by the exchange of the entire water molecule and, to a lesser extent, by proton 

or deuteron exchange. Parallel imaging of other nuclei will also be presented. 

(a)

MF75 

NMR IMAGING USING CIRCULAR SIGNALS IN THE SPATIAL FREQUENCY DOMAIN S 

S. Matsul, K. Seklhara, and H. Kohno 

Central Research Laboratory, Hitachi, Ltd. 

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

We demonstrate experlmentally a new type of method of imaging, in 

which siena1 measurements are taken during rotation of a field gradient. 

Detailed aspects of the method will be discussed in connection with 

unusual properties of the observed slgnal. 

Generally, the slgnal measured during the gradient rotation traces 

a circle in the spatlal frequency domain (so-called k space). I) Although 

the clrcular signal contains some information for imaging, it does not 

provide useful data that can be systematlcally and efficiently process- 

ed to yield a spin image. This is because the circle is not symmetric 

about the origin of the k space. However, if the center of the clrcle 

is approprlately shifted to the k origin, useful data can be obtained. 

The resultant signal directly provides symmetric circular phase infor- 

mation. The shift can be achieved by applying, amon E many ways, a sta- 

tionary fleld gradient prior to the rotation. The properties of such 

a circular signal are completely different from those of a usual FID 

slgnal. The unusual properties can be understood by expressing the 

clrcular signal in terms of Bessel functions of the first kind. 

The radius of the circle is given by 7G/WG, where Y is the gyromag- 

netic ratio, G denotes the gradient amplitude, and ~G is the angular 

frequency of the gradient rotation. Therefore, takin E measurements 

after changing either the gradient amplitude or the angular frequency 

permits a concentric set of clrcular signals with different radii to 

be obtained. The signal set can be converted to a spin image by suit- 

able data processing involving Fourier transformations along the radii 

and back projections. 

Reference 

I) S. Ljunggren, J. Magn. Reson. 54, 338 (1983). 

§ Published in part: S. Matsui and H. Kohno, J. Magn. Reson. 70, 157 

(1986).

MF77 

NMR IMAGING OF SOLIDS 

WITH A SURFACE COIL 

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

Chemistry Division, Code 6120 

Naval Research Laboratory 

Washington, DC 20375-5000 

A number of NMR techniques have already been 

demonstrated to be useful for imaging solids. These 

techniques are limited to small samples because 

traditional coil geometries require large amounts of 

power to generate the B 1 fields required for solid state 

imaging. The use of surface coils can somewhat 

circumvent this problem. 

Several imaging strategies are possible using 

surface coils, including rotating frame imaging and 

"depth" sensitive excitation. Because of line broadening 

in solids, resolution in the rotating frame experiment is 

a problem. Multiple pulse line-narrowing has been used 

for imaging solids; by virtue of its sensitivity to pulse 

amplitude/duration it is a form of depth sensitive 

excitation. Multiple pulse line-narrowing generally 

requires large B 1 fields thus limiting its use to regions 

very close to the surface coil. 

We will present several examples of surface coil 

imaging of solids employing multiple pulse line- 

narrowing. We will discuss the dependence of line- 

narrowing efficiency and depth sensitivity upon the 

multiple pulse technique. We also introduce the "magic 

angle nutation" sequence which is less sensitive to the 

magnitude of the B 1 field than traditional line-narrowing 

sequences.

MF79 

IMAGING AND IN WVO SPECTROSCOPIC APPLICATIONS 

OF COMPUTER OPTIMIZED PULSE SEQUENCES 

Francisco Loaiza and Warren S. Warren* 


Michael Silver 

Siemens Medical Systems, 186 Wood Ave. South, Iselin, NJ 

Computer optimization of entire pulse sequences, as opposed to 

individual pulses, generates substantial improvements in slice profiles 

for T2-weighted spin density images and other applications. 

Sensitivities to spin density or relaxation gradients are included in the 

optimization. We discuss the tradeoffs between different approaches to 

computerized pulse shape optimization, and present results of clinical 

trials which show peak power reductions and dramatically reduced 

distortions for multislice imaging. 

This work is supported by the National Institute of Health, the 

New Jersey Commission on Science and Technology, and Siemens 

Medical Systems. 

1. F. Loaiza, M. Levitt, M. McCoy, M. Silver and W. S. Warren, J. Chem. 

Phys. (submitted) 

2. F. Loaiza, K. T. Lim, M. Silver and W. S. Warren, J. Mag. Res. Med. 

(submitted)

MKI - POSTERS 

NNR STUDIES OF G-LACTALBU~IIN: 

MCTERIZATION OF A PARTIALLY UNFOLDED STATE 

J. Baum, C.M. Dobson, C. Hanley 




P.A. Evans 

Middlesex Hospital Medical School 

London, ENGLAND 

To understand the folding mechanism of proteins, it is 

important to characterize, at the molecular level, the 

structures of states intermediate between the folded and 

unfolded conformations. Incompletly folded proteins tend to 

have very small IH chemical shift dispersions, therefore 

methods have been developed to probe these intermediate states 

indirectly via the well-resolved IH spectrum of the native 

protein. Guinea-pig ~-lactalbumin provides an especially 

favourable system for the investigation of folding due to its 

sensitivity to solution conditions; within certain ranges of pH 

and temperature there exists a stable partially unfolded 

intermediate which we can study by NMR. PH-jump hydrogen 

exchange experiments are being developed to assign indirectly, 

through the native protein, the labile protons of the unfolded 

state, and magnetization transfer experiments are used to 

correlate the resonances of the unfolded protein with those of 

the native protein. These and other experiments have allowed 

us to identify regions of localized structure at the individual 

residue level in the unfolded form of ~-lactalbumin.

MK3 

OLIGONUCLEOTIDE STRUC'I13RE ~ BASED ON QUANTITATIVE 2DNOE SPECTRA 

Brandan A. Borgias* and 'rnomas L. James 

Department of Pharmaceutical Chemistry 

Unive~ty of California, San Francisco, CA 94143 

The use of 2DNOE (two-dimensional nuclear Overhauser effect) spectroscopy in the muc- 

characterization of biomolecules has generally been qualitative or semi-quantitative. 

Observed cross-peaks me presumed to be a consequence of the close proximity (< 5 ~,) for the 

associated protons. Distances are estimated based on the relative intensifies and buildup of cross- 

peaks according to an approximate relationship between the intensifies and the proton-proton dis- 

tances. Distances obtained in this manner have proven useful as constraints in structural determi- 

nations by distance geometry ! and molecular dynamics 2 calculations. 

The exact relationship between the inter-proton distances and the intensities is given by the 

exponential function: 

aCt=a) = exp(-RCm) ; 

where R is the relaxation matrix. The off-diagonal elements of the relaxation matrix are propor- 

tional to I/rij6 • 

Rij - 0.l,yi2 7j 21~[6J(o~ i + ~j) - J((0 i - ¢~j)] / rij6. 

Thus, for short mixing times (Zm---~), the inter-proton d i ~ can be estimated from the cross- 

peak intensities. At longer mixing limes this approximation breaks down due to spin diffusion. 

However, it is with mixing times of intermediate duration where one begins to observe a reason- 

able number of cross-peaks with acceptable signal/noise. 

In contrast to the approximate approach, exact intensities can be calculated for a given 

three-dimensional array of pmtom after diagonalizing the relaxation matrix: 

= exp(- ; 

where ;L is the diagonal eigenvalue matrix and ~ is the associated matrix of eigenveaors? We 

have incorporated this exact calculation of intensifies into a least-squares program which refines 

oligonucleotide structure. In the course of this work we have investigated the consequences of 

errors in the data on the refinement process. The major conclusions to be drawn are the foUowing. 

(1) ConsWaints are necessary. Refinement of the proton "smmure" in 3-space, without con- 

straints due to the molecular skeleton, is unsuccessful. In our approach each nucleotide 

is defined by ten parameters: 3 translational coordinates and 3 Euler angles for the whole 

nucleotide, 2 internal torsion angles (the glycosidic and C4'--C5' bonds) and the sugar 

pucker phase and amplitude. The phosphodiester linkages are not included. 

(2) Errors in diagonal peak intensifies (easily approaching 50% in the case of overlap) utterly 

destroy the refinement if they are included in calculation of the residuals. However, if 

the diagonals are ignored completely, the refinement is successful. 

(3) The correlation times can be successfully refined. 

References 

(1) Kline, A. D.; Braun, W.; Wfithrich, K. J. Mol. Biol. (1986) 189, 377-382. 

(2) Clore, G. M.; Gronenbom, A. M.; Brfinger, A. T.; Karplus, M. J. Mol. Biol. (1985) 186,435-455. 

(3) Keepers, J. W., James, T. I.. J. Magn. Reson. (1984) $7, 404-426.

MK5 

Abstract: 28th ENC, Asilomar, CA. April 5- 9, 1987 

INTERNUCLEAR DISTANCES AND CORRELATION TIMES FROM TRANSVERSE AND 

LONGITUDINAL CROSS-RELAXATION RATES 

Donald G. Davis, NIEHS, PO Box 12233, Research Triangle Park, NC 27709 

A novel method for determining correlation times and proton- 

proton distances for molecules in solution is demonstrated. These 

experiments may be done at a single field strength and require no 

priori assumptions about fixed internuclear distances or the cor- 

relation functions for different pairs of spins in the molecule. 

The success of the method is based on the fact that the longitudinal 

(~111) and transverse ((~'~) cross-relaxation rates have different 

dependencies on ~c such that in the range Ilog~dR~l, the ratio of 

(~lltO ~goes from 1.0 to -0.5. Accurate measurements of ~require 

that careful attention be given to offset corrections and to mini- 

mizing Hartmann- Hahn cross-polarization(I). Experimental details and 

data analysis for the determination of internuclear distances and 

correlation times of the cyclic peptide Gramicidin-S in DHSO-d 6 will 

be shown. 

References: A. Bax and D. G. Davis, J. Hagn. Reson. 6~, 207-213,(1985).

MK7 

IMPROVEMENTS OF THE 2D TRANSFERRED NOE EXPERIMENT AND APPLICATION IN THE 

CONFORMATIONAL ANALYSIS OF INHIBITORS BOUND TO CMP-KDO SYNTHETASE 

Stephen W. Fesik* , Edward T • Olejniczak • and William E • Kohlbrenner • 

Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064. 

Transferred nuclear Overhauser effects (TRNOE) provide a useful means of 

determining the conformation of enzyme-bound ligands. However, in the 2D 

version of the experiment certain precautions must be taken to alleviate some 

of the problems associated with the experiment• One of the problems is the 

presence of large protein signals which, in many cases, obscures the 

resonances of the ligand. In order to suppress these unwanted signals, we 

have taken advantage of the shorter spin-spin relaxation times (T 2) of the 

protein signals compared to the averaged signals of the ligand. This was 

accomplished by inserting a Carr-Purcell-Meiboo m-Gill pulse sequence before 

the evolution time (t 1) of the conventional 2D NOE experiment, markedly 

improving the quality of the spectra. Another problem, the presence of large 

zero quantum peaks, were eliminated by standard means, maintaining a constant 

1 

mixing time. 

The modified 2D TRNOE experiment described above was applied in the study 

of the bound conformations of CMP-KDO synthetase inhibitors. These studies 

were aimed at providing conformational information towards the design of more 

potent inhibitors of lipopolysaccharide biosynthesis and the development of a 

new class of antibiotics• Based on 2D TRNOE experiments using several 

inhibitors, it was found that their bound conformations depended on the 

hydrophobicity of their side chains. The bound conformations were used to 

propose the location of a hydrophobic and hydrophilic binding site. 

1. S. Macura, K. Wuthrich, and R.R. Ernst, J.Magn. Reson., 4__7_7, 351 (1982).

MK9 

A 2D-EXCHANGE SEPARATED LOCAL FIELD (EXSLF) EXPERIMENT 

K. Takegoshi* and C.A. McDowell, Department of C~emistry, 

University of British Columbia, 2036 Main Mall, Vancouver, British 

Columbia, Canada, V6T I¥6. 

Rate constants for the flip-flop spin exchange process 

between a IN spin coupled with a '~C spin and the surrounding 'H 

spins were determined in the absence perturbing rf fields, and also 

under the influence of both 'H and '*C rf fields. To determine the 

flip-flop rate in the absence of the rf fields, we developed a new 

technique, the Exchange Separated Local Field (EXSLF) experiment. 

The EXSLF experiment was applied to the CH group in a single crystal 

of dimedone, for two different orientations relative to the static 

magnetic field. The inverse of the flip-flop exchange rates 

determined by the EXSLF experiments are 276 and 391 ~s for the 

orientations Bo//b and Bo//C*, respectively. 

The flip-flop exchange motion under the influence of both 'H 

and '~C rf fields was also studied by examining the transient 

oscillation phenomena occuring during a spin-locking 

cross-polarization experiment. The values obtained for the inverse 

of the rate constants for the flip-flop exchange motion were 450 and 

540 ,s for Bo//b and Bo//C*, respectively. The observed slow 

flip-flop rate shows that the IH-'3C coupled spin system in a single 

crystal of dimedone is isolated from the surrounding 'H spins.

MKI1 

THE STRUCTURE OF THE SUBTILISIN INHIBITOR 2 FROM BARLEY DETERMINED 

BY IH-NMR SPECTROSCOPY, DISTANCE GEOMETRY CALCULATIONS AND 

RESTRAINED MOLECULAR DYNAMICS. 

e 

Flemming M. Poulsen i) Mogens KJ~r l) and Marius Clore 2) 

i) Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, 

DK-2500 Copenhagen Valby, Denmark 

2} Max-Planck-Institut f~r Biochemie, D-8033 Martinsried bei M~nchen, 

Federal Republic of Germany 

The barley subtilisin inhibitor is a protein of 83 residues, homologous 

to leech eglin c. The structure of the C-terminal part of the protein 

consisting of 65 residues has been studied using 2D-NMR techniques. The 

secondary structure has been determined, and consists of three short 

stretches of antiparrallel ~-sheet one long stretch of parallel ~-sheet 

furthermore one helix of 12-13 residues and a long loop. 

On the basis of approximately 300 assigned NOE's the structure has 

been calculated using distance geometry calculations. Subsequently 

restrained molecular dynamics was used to refine the structure. 

The structure obtained from NMR data agree's well with the structure 

of the inhibitor determined by X-ray crystallography of the subtilisin- 

inhibitor complex.

MKI3 

2D NMR - PSEUDOENERGY APPROACH TO THE THREE-DIMENSIONAL 

STRUCTURE OF ACYL CARRIER PROTEIN 

T. A. Holak* and J. H. Prestegard* 

Department of Chemistry, Yale University 

New Haven, CT 06511 

A method for protein structure determination from two 

dimensional NMR cross-relaxation data is explored using a 77 

amino acid protein, acyl carrier protein. The method is based on 

an energy minimization with a molecular mechanics program (AMBER) 

and incorporates NMR distance constraints in the form of a 

pseudoenergy term that accurately reflects the distance dependent 

precision of NMR cross-relaxatlon data. When used in an 

indiscriminant fashion, the method has a tendency to produce 

structures representing local energy minima near starting 

structures, rather than structures representing a global energy 

minimum. However, stepwise inclusion of energy terms, beginning 

with a function heavily weighted by backbone distance 

constraints, appears to simplify the potential energy surface to 

a point where convergence to a common backbone structure from a 

variety of starting structures is possible.

MKI5 

NA-23 NMR-INVISIBILITY IN LIVING SYSTEMS: 

2D MULTIPLE QUANTUM NMR AND NUTATION DIMENSION EFFECTS 

S 

William D. Rooney , Thomas M. Barbara and 

Charles S. Springer, Jr. 

Department of Chemistry, State University of New York, 

Stony Brook, New York 11794-3400 

The Na + ion is ubiquitous in nature in both extent and 

amount. Its major, stable, isotope, 23Na (I00%), is magnetic 

and gives a strong NMR signal. However, It is well-known 

that, for living systems, a portion of this signal is not 

observed when high resolution acquisition conditions are 

employed. There is general agreement that this is due to the 

effects of microscopic electric field gradients on this 

quadrupolar (I = 3/2) nucleus. There are two mechanistic 

extremes: a homogeneous interaction in which fluctuations of 

these gradients average the frequencies of the satellite 

transitions (~i/2 to ~3/2) to the same value but drastically 

shorten their T2 relaxation times, and an inhomogeneous 

interaction in which these frequencies are widely dispersed 

because of variations in the orientation of these gradients 

in the magnetic field. We have undertaken to discriminate 

these extremes with two kinds of multiple pulse 2D NMR 

experiments. In one, the projection of the 2D spectrum onto 

the v, axis displays the forbidden double quantum NMR 

spectrum. In the other, the projection onto the wl 

axis displays the effective nutatlon (Rabi) frequency of the 

central transition (I/2 to -I/2). We have prepared mode] 

systems, mostly consisting of long chain alkyl sulfate 

esters, which exhibit each of the four possible types of 

23Na NMR spectrum: oriented (lyotropic) liquid 

crystalline (same as single crystalline), unoriented liquid 

crystalline ("powder pattern"), homogeneously relaxed, and 

extreme-narrowed. The second and third represent the two 

mechanistic extremes for NMR-invisibility possible in nature. 

Our two kinds of 2D NMR experiments easily discriminate the 

second and third spectral types in the ~2 dimension. 

Both experiments share the property of taking advantage of 

the strong, sharp, central transition. In recent studies, we 

have conducted these experiments on living systems. 

Supported in part from NIH GM 32125 and NSF PCM 84-08339.

MK17 

STRUCTURES OF DNA OLIGOMERS DETERMINED 

BY 2D NMR AND DISTANCE GEOMETRY TECHNIQUES. 

C~uan Wang* and Arthur Pardi 


Rutgers, The State University of New Jersey 

New Brunswick, NJ 08903 

The double stranded decamers d(~AATC'~) and d(GCGCGTGACG) have been 

investigated by 2D NMR. Three-dimensional smlcmres of these molecules were generated by 

distance geometry techniques using proton-proton internuclear distances derived from NOESY 

spectra. Proton resonance assignments were made for all nonexchangeable aromatic and C1'-C3' 

sugar protons, most exchangeable imino and cytosine amino protons, and many C4' and C5' sugar 

protons in these molecules. In both decamers more than 40 inter-base pair and 50 intra-base pair 

proton-proton distances were calculated fi'om build-up rates derived from NOESY spectra at multiple 

mixing times. This distance information was then used as input for a distance geometry program to 

generate three-dimensional structures of the oligomers in solution. Correlations between base 

sequence and local variations in the DNA smJctme will be discussed.

MKI9 

SEQUENTIAL INDIVIDUAL 1H NMR RESONANCES ASSIGNMENTS 

OF CARDIOTOXIN III FROM FORMOSAN COBRA VENOM 

(NaSa naja atra) 

• + 

C. Yu and T. H. Hseu 

Department of Chemistry, National Tsing Hua University, 

Hsinchu, Taiwan* 

Department of Life Science, National Tsing Hua 

University, Hsinchu, Taiwan + 

Cardiotoxin III is one of the membrane active proteins 

from Formosan cobra (Naja naja atra). It is a small basic 

single polypeptide consisting of 60 amino acid residues 

cross-linked by four disulfide bonds. The most characte- 

rized biological activity of cardiotoxins is the in vitro 

hemolysis of erythocytes. Nonetheless, details about the 

mechanism of cardiotoxin hemolysis remain inconclusive. 

Knowledge of the molecular conformation of cardiotoxins 

might be informative with regard to this common feature of 

functional properties of all toxins in this class. The 

assignments of IH NMR resonances is the first first step to 

probe the structure-functional relationship of carditoxin. 

The result of sequential assignment of IH NMR spectrum 

for cardiotoxin III from naja naja atra is presented. The 

assignments are based entirly on the amino acid sequence and 

2D NMR experiment on 400 MHz. The measurements were done in 

both H20 and D20. Phase-sensitive and double quantum filter- 

ing 2D techniques combined with solvent elimination routine 

proved to be useful, particularly those cross peaks closed to 

diagnol area (e.g. phe-13 and phe-25). The pH tetration 

curves were consistent with the aromatic resonances assigments 

of cardiotoxin III by 2D experiments.

MK21 

ASPECTS OF PROTEIN STRUCTURE DETERMINATIONS WITH NMR 

ERIK R,P, ZUIDERWEG*o DAVID G, NETTESHEIM AND 

EDWARD T, OLEJNICZAK 

NMR RESEARCH. ABBOTT LABORATORIES, ABBOTT PARK. ILLINOIS 

60064 

1H 2D NMR AND COMPUTER METHODS TO OBTAIN THE DATA NECESSARY 

FOR THE DETERMINATION OF THE 3D STRUCTURE OF PEPTIDES AND 

PROTEINS WILL BE DISCUSSED AND EXEMPLIFIED WITH RESULTS 

OBTAINED ON RECOMBINANT CSA, A 75 AMINO ACID PROTEIN. ToPics 

TOUCHED UPON WILL INCLUDE PHASE COHERENT DECOUPLING FOR 

SOLVENT SuPPREsSION, ZZ SPECTROSCOPY FOR COMPLETE 

"FINGERPRINTS", PRESATURATIONLESS HOHAHA SPECTROSCOPY OF 

PEPTIDES IN H20 SOLUTION AND PHASE SENSITIVE COCONOSY FOR 

AMIDE PROTON EXCHANGE STUDIES, SPECTRAL BASELINE DISTORTIONS 

AND COMPUTER BASED CORRECTION METHODS WILL BE DISCUSSED. 

STRATEGIES FOR NOE IDENTIFICATION IN CROWDED SPECTRA, SUCH AS 

THE UTILIZATION OF SPIN DIFFUSION, WILL BE ILLUSTRATED. THE 

USE OF THE DISMAN DISTANCE GEOMETRY PROGRAM BY W. BRAUN AND 

N. Go FOR THE 3D STRUCTURE DETERMINATION OF THIS PROTEIN WILL 

BE DESCRIBED AS WELL AS METHODOLOGY TO REFINE THE STRUCTURES 

OBTAINED.

MK23 

MATER SUPPRESSION TECHNIQUES FOR THE GENERATION OF PURE PHASE 

TWO-DIMENSIONALNMR SPECTRA 

Vladlmlr Sklenar* and Ad Bax* 

Laboratory of Chemical Physics, Natlonal Institute of Diabetes 

Digestive and Kidney Diseases, National Institutes of Health 

Bethesda,MD.20892 

A number of different approaches has been proposed for suppression of 

the intense H20 resonance in 2D NMR spectra of biological compounds. Most 

commonly one employs presaturatlon of the H~O resonance using a low power 

irradiation prior to the observation pulse. The main disadvantage of this 

method is that resonances of exchangeable protons may also be saturated. 

Selective excitation using pulse sequences which have a null at the water 

resonance avoids this problem. A large variety of different excitation 

schemes has been designed in recent years. However, all but the slmplest 

90x-T-90_x sequence yield spectra that require a large linear phase 

correction. The baseline roll that result from such a phase correction can 

lead to intense artifacts in phase sensitive 2D NMR spectra. 

A new approach is described for water suppression in one- and 

two-dlmensional NMRwhlch generates pure absorptive spectra that are free 

of baseline dlstorslons. This method involves the use of a 90x-~-90_x 

hard pulse as a read pulse followed by a 90~-k~-90.~ refocusing pulse 

which is phase cycled for obtaining the highest possible water 

suppression. Incorporation into several of the most popular 2D NHR 

experiments (NOESY, HOHAHA, ROESY, HMQC and COSY) is discussed in detail. 

Examples of this approach for selective water suppression are demonstrated 

by recording the 2D spectra of the decapeptide LH-RH and the Dickerson 

dodecamer in 90% H20.

MK25 

OPTIMIZATION OF QUANTITATIVE PERFORMANCE OF 

SPECTRAL ANALYSIS BY MINIMAL SAMPLING 

Jerome L. Ackerman* and Vikram Janakiraman- 

Department of Radiology, NNR Facility, 

Massachusetts General Hospital, Boston, MA 02114 

Minimal sampling is a non-Fourier method of spectral 

analysis in vhich the complex amplitudes of prespecified basis 

signals are extracted by an algebraic solution. The basis 

signals may be simple sine and cosine raves as in the discrete 

Fourier transform. Alternatively, they may be oscillations with 

finite decay rate, or they may be the FID's corresponding to 

arbitrary lineshapes or subspectra. The utility of this form of 

spectral analysis lies in the principle that for each unknown 

amplitude, only one sample of the signal need be obtained. This 

can greatly reduce the time of the data acquisition process and 

size of the data set in multidimensional acquisitions. 

For example, in the collection of a COSY tvo-dimensional 

data set from a compound vith tventy spectral lines in the normal 

one-dimensional spectrum, there are exactly tventy possible 

frequencies in each of the dimensions of the two-dimensional 

spectrum (ignoring the possible appearance of multi-quantum 

artifacts). It is therefore possible, using minimal sampling, to 

collect the two-dlmensional data set vlth only twenty samples in 

the first time dimension. (One could also collect only twenty 

samples of each FID, rather than the usual 512 or so, but that 

would not offer any significant savings in total acquisition 

time.) 

The drastic reduction in the total number of data values 

acquired would suggest that the algorithm would suffer from very 

poor signal-to-noise performance. Sovever, the actual 

performance is significantly better than one might at first 

suspect. Most importantly, we have found a specific procedure 

for optimizing the data collection process by maximizing the 

noise immunity of the matrix transformation which actually 

accomplishes the spectral analysis. 

We will present an algorithm for optimizing the 

quantitative performance of minimal sampling, and illustrate the 

results of this process for simulated and actual data. 

"Permanent address: University of Pennsylvania, 

Philadelphia, PA 19104

MK27 

QUANTITATIUN OF 1-D SPECTRA WITH LOW SIGNAL TO NOISE RATIO 

Sarah J. Nelson* and Truman R.,Bro~ 

Fox Chase Cancer Center, Philadelphia, PA 1911! 

A new method of analysing 1-V spectra with low signal to noise ratio has 

been developed. In contrast to other techniques of noise suppression such as 

the mtched filter and maximum entropy method, this provides an automatic 

quantitation of the spectrum. The output of the computer algorithm which 

implements the new method comprises estimates of (i) a slowly varying 

background component, (ii) the variance of random noise, (iii) peak positions, 

peak heights, peak areas and (iv) the predicted accuracy of the peak parameter 

estimates. The performance of the method has been investigated using a variety 

of simulated spectra with different types of background and a range of 

different peak heights and line widths. A comparison of the filtered spectra 

with those obtained using the matched filte~ and maximum entropy method 

demonstrated the advantages of being able to directly estimate the variable 

background and to use both peak height and peak width in distinguishing peaks 

from random noise. The method has also been applied to a variety of different 

experimental data and shows distinct advantages over the conventional 

filtering techniques.

MK29 

ANALYS2D -GRAPHICS SOFTWARE FOR PROCESSING 

AND ANALYSIS OF 2D NMR DATA 

P. Darba* and L.R. Brown # 

Department of Biochemistry, University of Wisconsin-Madison, 

420 Benry Mall, Madison, WI-53706, U.S.A. 

and 

#Research School of Chemistry, The Australian National 

University, Canberra, A.C.T. 2601, Australia. 

ANALYS2D and its front-end package PROC2D are software packages used 

to process and analyze 2D NHR data on VAX and microVAX computers. 

Developed in FORTRAN77 and Tektronix PLOTIO GKS, it can be transported to 

other host computers with very little modification. PROC2D does the 

number crunching part of the operations such as 1D and 2D FFT, phase 

corrections, baseline corrections and display list generation. ANALYS2D 

provides for interactive analysis of 2D data including spin picking and 

bookkeepping of spin system data bases. 

PROC2D contains interactive routines for setting up 2D processing. It 

can be used in both interactive and batch processing modes. It is usable 

with both BRUKER and VARIAN data types and allows user defined 2D 

transform types like TPPI, States-Haberkorn-Ruben, absolute value and 

non-quadrature in e 1. It also includes auxillary programs that feature 

linear combination procedures for efficient generation of multiple 

quantum and multiple quantum filtered 2D NMR spectra. 

ANALYS2D has been mainly designed to replace the conventional method 

of analysis of 2D data using wall paper size plots, with the concept of 

interactive analysis of 2D spectra on a high resolution graphics 

workstation. It has menu driven architecture and features display of 2D 

contours, selective expansions of different regions, creation of spin 

system data bases, cursor based auto/manual spin picking, comparison of 

spin system connectivities between different data sets, comparison of 

experimental spin multiplet patterns with theoretical patterns and 

pattern library generation.

MK31 

SYMMETRY RECOGNITION APPLIED TO TWO DLMENSIOI~AL 

IH INMR SPECTRA OF PEPTIDES AND PROTEINS 

Jeffrey C. Hoch I", Flemming M. Poulson 2, 

Shen Hengyi 2, Mogens Kjaer 2, and Svend Ludvigsen 2 

I Rowland Institute for Science 

100 Cambridge Parkway 


2Chemistry Department 

Carlsberg Laboratory 

Gamle Carlsbergvej 10 

Valby, DENMARK DK-2500 

A hierarchical procedure which automatically locates features in two dimen- 

sional NMR spectra based on their symmetry properties is described. The pro- 

cedure makes use of projection operators derived from group theory. Results of 

the procedure applied to COSY data for the peptide hormone LHRH and barley 

subtilisin inhibitor protein are presented.

MK33 

DISPA-BASED RAPID AUTOMATED PHASING OF FT-NMR SPECTRA 

Edward C. Craig*, a and Alan G. Marshalla,b 

Department of Chemistrya 

(Department of Biochemistryb) 

The Ohio State University 

120 West 18th Avenue 


For a Lorentzian spectral peak, a plot of dispersion-vs.-absorption 

(DISPA) gives a circle, whose center is rotated about the origin by the 

angle~>(see Figure). In this poster, we will show that a rapid and 

convenient method for locating the center of the DISPA circle (and thence 

the phase misadjustment for that peak) is to locate the intersection of 

the perpendicular bisectors of two or more chords of the DISPA circle. 

Once the phase at the center of each of two or more peaks has been 

established, a linear (or quadratic) fit to a plot of~vs, frequency 

provides a smooth phase-correction function for all other spectral peaks. 

Automated phasing of carbon-13 FT-NMR spectra will be demonstrated. 

Imaginary 

/ 

Real 

! 

Frequency 

[This work was supported by the National Science Foundation 

(CHE-8218998) and The Ohio State University.] 

I. Marshall, A.G. (1982) "Dispersion versus Absorption (DISPA): Hilbert 

Transforms in Spectral Line Shape Analysis," in Fourier, Hadamard r 

and Hilbert Transforms in Chemistry, ed. A.G. Ma'rshall (P|enum, 

N.Y.), pp. 99-123.

MK35 

NETVORKING AND AUTOMATION IN THE HIGH-VOLUME LABORATORY 

by 

Stephen G. Spanton, Richard L. Stephens* and David ~Jhittern 

Department of Analytical Research, Abbott Laboratories 

North Chicago, Illinois 60064 

The linking of an NMR spectrometer equipped with an automatic sample 

changer to an external computer network has resulted in an extremely 

efficient system for the acquisition, processing and archiving of NMR 

spectra. Spectra of a large number of samples are acquired and saved on 

the ~ spectrometer using the sample changer. The external computer then 

fetches the raw data and (1) assigns each spectrum a reference number, (2) 

decodes and enters various information into an archival data base, and (3) 

saves the ray data on magnetic tape. Routine one-dimensional 1H spectra 

are then Fourier transformed, phased, referenced, scaled, integrated and 

plotted by the external computer operating in batch mode. In addition, 

software has been developed at Abbott to alloy the interactive processing 

and plotting of one-dimensional spectra by chemists (and spectroscopists) 

using the computer network and graphics terminals located in their ovn 

laboratories.

MK37 

IMPROVEMENT OF INVERSE CORRELATION EXPERIMENTS BY SHAPED PULSES 

W. Bermel* a), C. Griesinger* b) , S. Steuernagel c), 

K. Wagner c), H. Kessler c). 

a) Bruker Analytische Messtechnik GmbH, Silberstreifen, 

D-7512 Rheinstetten 4, West Germany 

b) Laboratorium fur physikalische Chemie, ETH-Zentrum, 

CH-8Og2 ZUrich, Switzerland 

c) Institut fur organische Chemie, J. W. Goethe Universit~t, 

Niederurseler Hang, D-6000 Frankfurt/M, West Germany 

Correlation experiments via heteronuclear long range couplings provide 

useful information for the assignment of resonances and about connec- 

tivities of substructures in oligopeptides and other classes of organic 

and bioorganic compounds. 

The corresponding inverse experiment, which has a better signal to noise 

ratio than conventional techniques, has been introduced recently 1). For 

the application to peptides mainly the carbonyl carbons which cover a 

small range of chemical shifts in F 1 are of interest, whereas the whole 

proton spectrum is required in F 2. 

The selection of a small frequency window in the F 1 dimension is there- 

fore a prerequisite to obtain sufficient digitization with a reasonable 

amount of tl-values. This can be done with semiselective pulses. We used 

Gaussian shaped pulses for this kind of semiselective 2D experiments. 

The reduction of the F 1 frequency range of more than 10 kHz to a few 

hundred Hz results in a considerable resolution gain. The sensitivity is 

also improved due to good digitization. 

Modifications of the basic sequence will be discussed, which allow to 

adjust the experiment to one's needs: either to obtain a maximum number 

of correlation peaks or to derive qualitative information about the size 

of heteronuclear coupling constants. 

1) L. MUller, J. Am. Chem. Soc 101, 4481 (1979); 

A. Bax, R. H. Griffey and B. L. Hawkins, J. Magn. Reson. 55, 

301 (1983)

MK39 

A Partial Excitation Method in Two-dimensional Nuclear Mag- 

netic Resonance Spectroscopy Using a Tailored Pulse Having 

a Sinc Function Shape 

Muneki Ohuchl, Kazuo Furlhata~ and Haruo Seto~ 

JEOL Co., Nakagami, Akishima, Tokyo, ~lnstitute of Applied 

Microbiology, University of Tokyo, Bunkyo-ku, Tokyo, Japan 

Two-dimensional (2D) NMR spectroscopy has a disadvantage 

that cross-peak patterns can not be analyzed in detail due 

to the low digital resolution caused by the limited capacity 

of data memory and by the limited measurement time. This 

shortcoming can be eliminated by measuring a narrow spectral 

region using partial excitation pulses. A slnc function 

pulse can excite signals within a narrow frequency range, 

while the side lobes produced from a rectangular pulse ex- 

cite undesirable neighbor signals outside the range. 

We have developed the partial excitation method in 2D NMR 

spectroscopy[l] by using a tailored pulse produced from a 

sinc function type pulse, and the digital resolution of 2D 

NMR spectra has been enhanced several times by using this 

method. Increased digital resolution allows recognition of 

cross-peak patterns and coupling constants can be determined 

from their patterns. 

In this paper, application of this method to COSY and 

HMBC[2](Heteronuclear Multiple Bond Connectivity) will be 

reported. 

I) M.Ohuchi et.al., J.Magn.Reson. in press. 

M.Ohuchl et.al., 25th NMR Conference Tokyo (1986) 

2) A.Bax et.al., J.Am.Chem. Soc., I08 2093 (1986)

MK41 

PARAHYDROGEN AND SYNTHESIS ALLOWS 

DRAMATICALLY ENHANCED NUCLEAR ALIGNMENT 

C. Russell Bowers* and Daniel P. Weitekamp 

Arthur Amos Noyes Laboratory of Chemical Physics 

California Institute of Technology 127-72 

Pasadena, CA91125 

Molecular hydrogen is known to come in two forms, para-H2 and 

ortho-H2, which differ from one another in their nuclear spin states. A 

consequence of the symmetrization postulate of quantum mechanics is that 

these two forms are associated only with specific states of molecular rotation. 

In particular, the lowest energy rotational state has the para nuclear spin 

state, (1/2)t(]a~ >-ilia > ), so that low-temperature equilibration prepares the 

protons predominantly in this non-magnetic state. This para-H2 may be 

used even as a room temperature reagent, since conversion to the ortho form 

is slow in the absence of a catal' y st. 

This poster presents the ~irst experimental demonstration of the recent 

prediction1 that the nuclear spin order ofpara-H2 can be converted by 

chemical reaction into large v nonequilibrium NMR signals. The reaction 

studied is the molecular addition of H2 to acrylonitrile to form propionitrile. 

The reaction is performed in deuterochloroform solution in a standard NMR 

tube at room temperature and pressure with the aid of Wilkinson's catalyst, 

tris (triphenylphosphine) rhodium(I) chloride. The hydrogenation is initiated 

by bubbling H2 gas through the solution containing acrylonitrile and catalyst. 

If the gas has been enriched inpara-H2 by previous exposure to a 

paramagnetic catalyst in liquidnitrogen, a n/4 pulse elicits an f.i.d, whose 

Fourier transform shows antiphase multiplets at 'the expected propionitrile 

frequencies as shown in)artn par~ ~a) of the figure. The amplitude of these lines is at 

least two orders of magnitude greater than would result from the equilibrium 

magnetization of the product formed. This is evidenced by the absence of 

observable product signal in part b), obtained after a delay of several times T1, 

even though the product is chemically stable. 

(o) 

(b) 

f i ~ | 

I I I 

6 3 0 

~ ) C.R. Bowers and D. P. Weitekamp, "rhe Transformation of 

ppm 

ymmetrization Order to Nuclear Spin Magnetization By Chemical 

Reaction and NMR", Phys.Rev.Lett. 53, 2645 (1986).

MK43 

MjECHANIStCSOFCOHEREHCETRANSFER IN LIQUIDS: 

=ANTIPHASEmARD "IMPBASE" TRANSFER 

Renzo Bazzo, Jonathan Boyd, Nick $offe 

Department of Biochemistry, University of Oxford 


Many NNR experiments, both 1 and 2 dimensional, rely on a 

common mechanism of coherence transfer, between weak]y coupled 

nut]el, which is referred to as the "antiphase" mechanism. 

Free evolution can be described as a continuous exchange 

between inphase and anciphase terms; whereas pu]ses (usual]y 

assumed to be non-selective) cause coherence transfer of 

antiphase terms or give rise to multiple quantum coherences. A 

simple geometrical model will be presented which is useful to 

represent the above processes. 

Cross polarization experiments, introduced for liquids by 

Braunschweiler and Ernst and further developed by 8ax and Davis 

can give rise to "inphase" or net coherence transfer. We shall 

present an analysis of the coherence transfer mechanism 

involved in this class of experiments. 

The cross polarization experiment will be compared with 

other two-dimensional correlation techniques which rely 

completely upon the antiphase mechanism. The two mechanisms of 

coherence transfer will be contrasted.

MK45 

SIMULTANEOUSLY OBSERVING THE HOMONUCLEAR 

AND HETERONUCLEAR EDITED SIGNALS WITHOUT 

AN X NUCLEUS DECOUPLER 

T. Jue 

Dept. of Mol. Biophysics and Biochemistry 

Yale University 


The promise of sensitivity enhancement has spurred research 

efforts to edit the *H NMR spectrum. For in vivo studies, the 

metabolic pathways have been followed with ,3C precursors, but 

can be followed with enhanced sensitivy with |*sc}-*H editing 

strategies. In particular, the one dimensional techniques based 

on J modulation behavior have yielded successful results in 

brain, liver, and muscle experiments. However, these extant 

methods yield only the edited *3C-*H signals upon subtraction of 

the alternate, modulated spin-echo experiments, but do not 

necessarily give edited *2C-*H signals upon addition -- only the 

overall *2C-*H resonances which are often encumbered with the 

endogenous background lipid signals. 

But in vivo studies require both the *2C-*H and *3C-*H 

signals to probe the important question of specific activity, 

which is posed by the various sources of a metabolic pool. 

Consequently, we have devised a simple scheme to simultaneously 

obtain both the homonuclear and heteronuclear edited signals 

without a *sc decoupler. Pivotal metabolites are amenable to 

such a winnowing scheme.

MK47 

AN IMPROVED CHORTLE PULSE SEQUENCE 

GERALD A. PEARSON 

CHEMISTRY DEPARTMENT, UNIVERSITY OF IOWA 

IOWA CITY, IOWA 52242 

We have developed s pulse sequence which substantially 

improves the accuracy and resolution of the CHORTLE (I) 

experiment. (Carbon-Hydrogen correlations from One- 

dimensional polaRization-Transfer spectra by LEast-squares 

analysis) One can now adjust tCH, the net evolution time 

for dcm prior to polarization transfer, independently o£ 

tM,max, the maximum net evolution time for proton chemical 

shift, 6H. Using tN,max m 10 msec, CHORTLE now routinely 

measures 6H with an error ~(~H) ~ I HZ, and resolves non- 

equivalent geminal methylene protons whose chemical shifts 

differ by only 30 Hz. Exploratory CHORTLE experiments with 

longer tH,max have achieved ¢(6H) ~ 0.2 Hz in favorable 

cases, and it should be possible to achieve ~(6H) s 0.02 Hz 

in special cases, with a IH spectrum width ~ 5000 Hzl 

In its orlElnal form, the CHORTLE experiment typically 

yielded ~(6H) ~ 3 Hz, end frequently could not resolve non- 

equivalent gemlnal protons whose chemical shifts differ by 

less than about 70 Hz. This was because tM.max = tCH, and 

tcH is restricted to values which optimize the polarization- 

transfer efficiency. With tcH ~ I/2JcH, tH,max was only 3.2 

meec. Tzeng(2) pointed out that it is possible to 

circumvent this limitation by setting tcH = 3/2JcH, 5/2dcs, 

etc., in exactly the same way that Reynolds and others TM 

re-parameterized the COLOC c4) sequence. Unfortunately, 

increasing tcs has three disadvantages. First of all, 

errors arising from unwanted long-range polarization 

transfer remain approximately constant, rather than 

decreasing with increasinE tH,ma,. Secondly, the desired 

polarization-transfer efficiency becomes more sensitive to 

the value of Jcs; since Jcs can vary from 118 Hz to 220 Hz 

or more in some samples, this will inevitably lead to loss 

of sensitivity for some signals. Finally, only certain 

values of ts,max are possible (ca. 10 msec, 16.5, 23, ...) 

with this approach. The new pulse sequence permits one to 

choose ts,max to be a truly optimum compromise between 

desired accuracy and the sensitivity losses caused by IH 

relaxation and IH multiplet dephasing arising from IH-IH 

coupling. 

1. G.A.F~Ju~SON, J.~oN.RZSON. 6,4, 48T (1~). 

2. C.S.TzENo, UNIV. (:~ C~U-IF. AT RI~ERSI2* I~IVATI[ CC]I,~I~.ATION. 

3. W.F.REYNOLDS, D.W.HUOMES, M.I~A,'XOK-I~, AND R.G.EN~xOUEZm 

J.I'IAoN.RZ~w~N. 64, 304 (1985). 

4. H.I~S~.~R, C.CW~IESI~R, J . ~ ( ~ , AND H.R.I-~I, 

J.MA(Nw. REIwmw. 6"/', 331 (1~34).


W 

2:00- 5:00 

Wednesdayj April 8j 1987

o 

°~ 

tO. 

o 

.9,o 

Kiln - Poster Session Layout 

WK8 r] 

Flynn ~ 

Mg7 

Fesik II 

WK6 

Fesik 

MK5 

Davis 

WK4 

Brown 

MK3 

Borgias 

WK2 

Bogusky 

MK1 

Baum 

Chalkboard 

MK9 WK2 MK25 WK44 MK41 

Takegoshi Sute Ackerman Warrer Bowers 

WK10 MK2:, WK26 MK3. ¢ WK42 

McLennan $klenka Barker Ohuch Bodenhausen 

MK11 WK2: MK27 WK3E MK43 

Poulsen Levltl Nelson Mac Boyd 

WK12 MK21 WK28 MK37 WK44 

Mlrau Zuiderw~ Brown Bermel Coxon 

MK13 WK2¢ MK29 WK36 MK45 

Holak Ziessow Darba Tang Jue 

WK14 MK19 WK30 MK35 WK46 

Snrensen Yu Grahn Stephens Meyerhoff 

MK15 WK18 MK31 WK34 MK47 

Rooney Narula Hoch Picart Pearson 

WK16 MK 17 WK32 MK33 WK48 

Hiyama Wang Johnson Craig F:lance

Firelight Forum - Poster Session Layout 

WF10 

Chu 

MF9 

Williamson 

WF8 

Pines 

MF7 

Eckert 

WF6 

Kay 

MF5 

Pekar 

WF4 

Lamb 

MF3 

Gonen 

WF2 

LaMar 

MF1 

Allen 

MF11 

Beshah 

WF12 

Bork 

MF13 

Bryant 

WF14 

Bryant 

MF15 

Carduner 

WF16 

Duncan 

MF17 

Ead 

WF18 

Dec 

MF19 

Jiang - 

WF20 

Jakobsen 

WF30 

Nissan 

MF29 

Merrill 

WF28 

Wind 

MF27 

Quinting 

WF26 

Limbach 

MF25 

Hill 

WF24 

Campbell 

MF23 

qleason 

WF22 

Hartzell 

MF21 

Garbow 

MF31 

Oldfield 

WF32 

Opella 

MF33 

Roberts 

WF34 

Simonsen 

MF35 

Stebbins 

WF36 

Vander- 

Hart 

MF37 

Williams 

WF38 

Lock 

MF39 

StOcklein 

WF40 

Jarvie 

Chalkboard I 

Tsang Kopelevich 

MF49H WF52 

Ronemus Maple 

WF,~ MFS3 

Muir'] Jarrel 

MF47HWF54 

Nicholson ~lOmlch 

MF55 

Johnston 

MF45, H WF56 

Brandes Mattingly 

WF=I] "~ 

Santini Bendall 

MF43, n WF58 

Johnson Black- 

ledge 

MF59 

Briggs 

MF41 ~ WF60 

Behling Thoma 

Kormos Lowe 

Keller MF~911W~2 Hetherington 

WF6811MF73 

amesi i Mateescu 

MF°'IIW ' 

Schmal- Karczmar 

brock 

WF6611MFTS 

offrionl I Matsui 

MF~IIW~' 

Garwood Metz 

V-EUtlM~ 

Dumoulin Miller 

MF~IIWF~B 

Dixon Saarinen 

WF62 H MF79 

Cockman Warren 

MF"IIWF~O 

Brown Szeverenyi 

Women's Rm Men's Rm 

~) 

(J 

03 

.m 

LI. 

E3 

o

WF02 

WF04 

WF06 

WF08 

WF10 

WF12 

WF14 

WF16 

WF18 

WF20 

WF22 

WF24 

WF26 

WF28 

Presenter 

LaMar, G. N. 

Lamb, D. M. 

Kay, L. E. 

Pines, A. 

Chu, S. C.-K. 

Bork, V. 

Bryant, R.G. 

Duncan, T. M. 

Dec, S. F. 

Jakobsen, H. J. 

Hartzell, C. J. 

Campbell, G. C. 

Limbach, H.-H. 

Wind, R. A. 


Wednesday, April 8, 1987 

Title 

Utility of Nuclear Overhauser Experiments in the 

Study of Heme Proteins 

Fixed Field Gradient NMR Diffusion Measurements 

Using Bessel Function Fits to the Spin-Echo Signal 

Motional Properties from Forbidden Peak Intensities in 

Double Quantum Spectra of Macromolecules 

Multiple Quantum and 129Xe NMR Studies of the 

Distribution of Molecules in a Zeolite 

Bulk Magnetic Susceptibility Effects in 23Na NMR 

Spectra of Compartmentalized Samples Containing 

Na ÷ and Shift Reagents 

Determination of Enzyme-Steroid Binding Sites by 

CPMAS 13C NMR and Selective Excitation 

The Use of Multiple Echo Acquisition and Stimulated 

Echos to Detect Slow Motion 

Characterization of Transition Metal Silicides with 29Si 

NMR Spectroscopy 

High-Speed MAS 19F NMR of Fluorocarbon 

Polymers 

Design of an Efficient Probe for High Field 

Multinuclear CP/MAS NMR of Solids 

Orientation of the 15N Chemical Shift Tensor in a 

Polycrystalline Dipeptide 

VT CP/MAS NMR of Antiferromagnetic Metal 

Complexes 

Temperaturevariable Solid Solution CPMAS NMR 

Studies of Dyes in Glassy Polymers 

Dynamic Nuclear Polarization in Organic Conductors 

Location Numbering Scheme: W for Wednesday, F for Firelight Forum, 

K for Kiln followed by the Poster number. Boldfaced type for featured 

posters.

WF30 

WF32 

WF34 

WF36 

WF38 

WF40 

WF42 

WF44 

WF46 

WF48 

WF50 

WF52 

WF54 

WF56 

WF58 

WF60 

WF62 

WF64 

Presenter 

Nissan, R. A. 

Opella, S. 

Simonsen, D. M. 

Vander Hart, D. L. 

Lock, H. 

Jarvie, T. P. 

Hornak, J. P. 

Santini, R. 

Beshah, K. 

Muira, H. 

Tsang, P. 

Maple, S. R. 

Bliimich, B. 

Mattingly, M. 

Blackledge, M. J. 

Thoma, W. J. 

Cockman, M. D. 

Dumoulin, C. L. 

Title 

Solid State 31p MAS NMR as a Tool for Studying 3- 

Dimensional Solids: The Chalcopyrites ZnSiP2, 

ZnSnP2, ZnGeP 2 and Related Materials 

Solid State NMR of Proteins 

13C MAS NMR Studies of Various Supported Metal 

Catalysts 

A Proton MAS NMR Method for Determining Intimate 

Mixing in Polymer Blends 

29Si Dynamic Nuclear Polarization Studies of 

Dehydrogenated Amorphous Silicon 

Nonaxially Symmetric Dipolar Couplings in Solids and 

Liquid Crystals 

Errors in Mapping RF Magnetic Fields 

Proton Detected 31 p_ 1H HETCOR of DN A Frag men ts 

Deuterium NMR Study of Methyl Group Dynamics in 

L-Alanine 

Segmental Dynamics in Nylon 66 by Deuterium NMR 

Solid State NMR Dynamics Studies of Duplex RNA 

Analysis of Complex Mixtures by Ultrahigh 

Resolution NMR 

2D Exchange NMR in Non-Spinning Powders 

Localized Proton Density, Relaxation Times and Self 

Diffusion Coefficient Measurements in Single Cells 

by NMR Microscopy 

Spatial Localisation of 31p NMR Spectroscopy using 

Phase Modulated Rotating Frame Imaging 

Sensitivity of Surface Coils to Deep Lying Volumes 

Convolution Chemical Shift Imaging 

NMR Flow Imaging 



posters.

WF66 

WF68 

WF70 

WF72 

WF74 

WF76 

WF78 

WF80 

WK02 

WK04 

WK06 

WK08 

WK10 

WK12 

WK14 

WK16 

Presenter 

Geoffrion, Y. 

James, T. L. 

Kormos, D. W. 

Hetherington, H. P. 

Karczmar, G. S. 

Metz, K. R. 

Saarinen, T. R. 

Szeverenyi, N. M. 

Bogusky, M. 

Brown, S. C. 

Fesik, S. W. 

Flynn, P. F. 

McLennan, I. J. 

Mirau, P. A. 

SOrensen, O. W. 

Hiyama, Y. 

Title 

Immobilized Ferrite Particles: Selective Spoiling of a 

Homogeneous B 0 Field and Its Application to 

Surface Coil Spectroscopy 

The SWIFT Method for In Vivo Localized 

Spectroscopy 

Natural Abundance Carbon- 13 NMR Imaging in 

Biological Systems 

The Description and Elimination of Subtraction 

Artefacts in 1H Editing Schemes: A Phase Cycling 

Scheme to Eliminate Absorptive and Dispersive 

Errors 

Tailored Excitation in the Rotating Frame 

Rapid Rotating-Frame Imaging 

A Novel Method for Diffusion and Flow 

Measurements: Imaging of Transient 

Magnetization Gratings 

Multiple Quantum Filtering: Uses in Imaging and 

Imaging Related Experiments 

15N NMR of Macromolecules: Applications to the 

Study of Proteins in Solution 

P. E. COSY, Double Quantum Filtered Relay 

Spectroscopy and More 

Isotope-Filtered Proton NMR Experiments for 

Simplifying Complex Spectra 

Isotropic Mixing in DNA 

1H, 13C and 15N NMR Studies of Metal Complexes of 

Bleomycin 

Quantitative Interpretation of a Single 2D 

NOE Spectrum 

Symmetry and Antisymmetry in 2D NMR 

Spectra 

Multinuclear Solid State NMR Studies of Internal 

Molecular Dynamics in Fibrous and Crystalline 

Proteins 



posters.

WK18 

WK20 

WK22 

WK24 

WK26 

WK28 

WK30 

WK32 

WK34 

WK36 

WK38 

WK40 

WK42 

WK44 

WK46 

Presenter 

Narula, S. S. 

Ziessow, D. 

Levitt, M. H. 

Suter, D. 

Barker, P. B. 

Brown, L. R. 

Grahn, H. 

Johnson, B. A. 

Picart, F. 

Tang, J. 

Mao, J. 

Warren, W. S. 

Bodenhausen, G. 

Coxon, B. 

Meyerhoff, D. J. 

Title 

2D NMR Methods for Spin System Identification in 

Large Proteins 

Recent Progress in Multidimensional Stochastic NMR 

Spectroscopy 

Solvent Suppression Without Phase 

Distortion 

Broadband Heteronuclear Decoupling in the Presence 

of Homonuclear Interactions 

Line Shapes in One-Dimensional Chemical Shift 

Imaging 

Selection of Coherence Transfer Pathways by Fourier 

Analysis: How to Improve the Efficiency of 2D 


Pattern Recognition in 2D NMR. A Multivariate 

Statistical Approach with Logic Programming 

Chemical Exchange in Metal Clusters. Analysis with 

2D Linear Prediction and Direct Analysis of the 

Rate Matrix 

Deconvolution of High Resolution Two-Dimensional 

NMR Signals by Digital Signal Processing with 

Linear Predictive Singular Value Decomposition 

Linear Prediction Z-Transform (LPZ) Spectral 

Analysis with Enhanced Resolution and Sensitivity 

Experimental Study of the Optimized Selective RF 

Pulses 

Pulse Shaping for Solvent Suppression and Selective 

Excitation in Two-Dimensional and Multiple Pulse 


Relaxation-Allowed Coherence Transfer Between 

Spins Which Possess No Mutual Scalar Coupling 

Two-Dimensional POMMIE 13C NMR Spectrum 

Editing 

Multiple-Acquisition Two-Dimensional Homonuclear 

Shift Correlation Spectroscopy 



posters.

WK48 

Presenter 

Rance, M. 

Title 

Improved Techniques for the Acquisition of TOCSY 

and CAMEL,SPIN Spectra and Computer 

Simulations of the TOCSY Experiment 



posters.

WF2 

LrIII~ITY OF NUC].FAR OVERHAUSER EXPERIMENTS IN THE S'IXJDY OF 

]-IEME PROTEINS 

V. Thanabal, W. S. Smith, M. J. Chatfield, S. D. Emerson, 

J. L. McGourty, J. Hauksson, D. H. Peyton, J. T. J. Lecomte, 

K.-B. Lee, and G. N. La Mar* 

Dept. of Chemistry, University of California, Davis, CA 95616 

The paramagnetic center of heme proteins also contributes 

significantly to relaxation such that it becomes very difficult to 

saturate resonances which arise from protons near the iron without 

significantly perturbing the rest of the spectrum via off-resonance 

effects. In addition, the systems have high molecular weights, 

leading to the usual spin-diffusion effects. 

We have developed methods of using the nuclear Overhauser 

effect in paramagnetic hemoproteins in the light of the problems 

mentioned above. Included in this study are numerical solutions of 

the Bloch equations evaluating the off-resonance effects expected 

when using high saturating power on a system of fast-relaxing 

protons. Further, we provide examples of uses we have found for 

nuclear Overhauser effect studies in paramagnetic heine proteins 

with molecular weights ranging up to greater than 75,000.

WF4 

FIXED FIELD GRADIENT NMR DIFFUSION MEASUREMENTS USING 

BESSEL FUNCTION FITS TO THE SPIN-ECHO SIGNAL 

D. M. Lamb*, P. J. Grandinettl, and J. Jonas 


School of Chemical Sciences 

University of Illinois 

Urbana, Illinois 61801 

A new technique for diffusion measurement by NMR using a fixed fleld 

gradient is described. The method makes use of a Bessel function fit 

analysis to the spin-echo signal in order to determine both the applied 

gradient and the diffusion coefficient simultaneously. Results of tests 

of the method using water and benzene are presented, and the utility of 

the technique is demonstrated with a report of preliminary results for a 

determination of the diffusion of naphthalene dissolved in compressed, 

supercritical carbon dioxide.

WF6 

MOTIONAL PROPERTIES FROM FORBIDDEN PEAK INTENSITIES IN DOUBLE 

QUANTUM SPECTRA OF MACROMOLECULES. 

Lewis E. Kay*, T.A. Holak, and J.H. Prestegard 

Department of Chemistry, Yale University, New Haven CT., 06511 

Typical n quantum filtered one and two dimensional spectra 

consist of peaks associated only with spins having Kesolved 

scalar couplings to at least (n-l) equivalent or nonequivalent 

spins. Consider, for example, a methyl group connected to a 

tertiary carbon forming an A 3 spin system. On the basis of a 

simple theoretical formalism for multl-pulse experiments all 

peaks stemming from the single resonance associated with this 

system should be removed by a multiple quantum filter. Multiple 

quantum peaks associated with degenerate spin systems of this 

type do, however, appear in spectra of macromolecules. 1"3 Despite 

the potential pitfalls associated with interpretation of these 

additional resonances, their appearance, when properly 

understood, can provide useful information concerning the 

dynamics of the spin system involved and ultimately the 

structural properties of the parent molecule. This is due to the 

fact that the appearance of such forbidden peaks is a direct 

consequence of cross correlation effects between spins. 

We will present an investigation of the motional properties 

of an X 3 spin system found in mlcelles of deoxycholate using 

forbidden peak intensities from a one dimensional analogue of the 

double quantum 2D experiment. Applications to the AX 3 spin 

systems of alanine residues in proteins will also be discussed 

with an emphasis on how an understanding of methyl group dynamics 

can aid in interpretation of NOE cross peak intensities involving 

these groups. 

I. Muller, N; Bodenhausen, GI Wuthrich, K: Ernst, R.R. 

J. Magn Reson. 1985, 65, 531. 

2. Muller, N; Ernst, R.R; Wuthrich, K. J. Am. Chem. Soc. 1986, 

108, 6482. 

3. Rance, M; Wright, P.E; Chem. Phys. Letters 1986, 124, 572.

WF8 

MULTIPLE ~ANTUH AND 129XE NMR STUDIES OF THE DISTRIBUTION OF MOLECULES 

IN A ZEOLITE • 

R. Ryoo, S.-B. Liu, L. C. de Menorval, and A. Pines 


Proton multlple-quantum (MQ) NMR measurements and analyses of 129Xe 

NMR spectra were used to probe the spatial distrlbutlon of simple 

molecules adsorbed in molecular sleves. The behavior of homogeneously 

chemlsorbed hexamethylbenzene (HMB) In the supercages of Na-Y zeolite is 

demonstrated. Distinct chemlcal shift llnes were observed from 129Xe 

NMR spectra of adsorbed xenon on Na-Y zeolite samples with different wt% 

of ehemisorbed HMB molecules. In the absence of HMB chemisorbed in the 

sample, a single llne at - 90 ppm due to xenon (300 Tort) In zeolite 

supercages Is obtained. When, on the average, each zeolite supercage is 

occupied by one HMB molecule, a single line occurs at different chemical 

shift values (- 120 ppm). In the intermediate case, when only a portion 

of the supercages are occupied by the HMB molecule, both llnes are 

present corresponding to the two cases above. 

The clusterlng of HMB molecules In zeollte supercages has been 

confirmed by proton MQ NMR measurements. For samples below - 12 wig HMB 

In Na-Y zeolite, HQ NMR data glve conslstant results indicating that 

only up to one HMB molecule per zeolite supercage can occur. Thls Js In 

accord wlth the observations from 129Xe spectra. 

These techniques have proven to be useful in the first step toward 

understanding the behavior of molecules under restricted dimension. 

*R. Ryoo, S.-B. L1u, L.C. de Henorva], J. Fralssard and A. Pines. to be 

publlshed.

WFIO 

BULK MAGNETIC SUSCEPTIBILITY EFFECTS IN NA-23 NMR SPECTRA OF 

COMPARTMENTALIZED SAMPLES CONTAINING NA + AND SHIFT REAGENTS 

S 

Simon C-K. Chu , James A. Balschi, & Charles S. Springer, Jr. 

Department of Chemistry, State University of New York, 

Stony Brook, New York 11794-3400 

Since the Z3Na NMR signal is by far the second strongest 

arising from tissue samples in pulsed experiments, 

developments in 23Na NMR of living systems are occurring very 

rapidly. 23Na MRI has become the second most common (e.g., 

Magn. Res. Med., 3, 296, 1986). Because of the isochronicJty 

of Z3Na resonances from different compartments, we and 

several other groups introduced paramagnetic shift reagents 

(SRs) for use with Z3Na (and other cationic resonances) 

in 1981-82, and we reported the nature of the spectra arising 

from SR-perfused tissue in 1985 (BiophFs. J., 48, 159, 1985). 

The first report of 23Na spectra from a living animal 

infused wlth a SR has recently appeared (J. Magn. Res., 69, 

523, 1986). 

Different SRs cause hyperfine shifts of the Z3Na NMR 

signal of different magnitudes and different signs. The 

former is because of differing equilibrium quotients and 

limiting shifts (dipolar) in the different SR-Na ÷ binding 

equilibria. The latter is because of differing geometric 

relationships between the Na ÷ binding site(s) and the 

axes of the magnetic susceptibility tensor of the SR 

molecular anion. 

Since, in living systems, the distribution of the SR 

will be restricted to certain tissue compartments (e.g., 

vascular only, interstitial only, vascular and interstitial), 

bulk magnetic susceptibility (BMS) effects will be manifest 

in the 23Na NMR spectrum. Both the magnitude and the 

sign of the BMS shift depend on the shape of the compartment 

and its orientation with respect to the static magnetic field 

(B0). We have conducted a thorough comparison of the 

relative sizes of the BMS and hyperfine shifts induced by 

three different SRs in cylindrical compartments (simulating 

either blood vessels or interstitial spaces) oriented either 

parallel or perpendicular to the B0 field direction. 

For the SRs chosen, both the magnitude and the sign of the 

hyperfine shift also vary. Thus, the ratio of the BMS 

contribution to the hyperfine contribution varies over a very 

wide range (-0.92 to 0.75, in the samples chosen). These 

contributions are, of course, algebraically additive in any 

given spectrum. The local inhomogeneJties produced outside a 

cylindrical vessel running perpendicular to B0 also 

cause interesting inhomogeneous broadening patterns in the 

resonances of nuclei restricted to the space outside the 

vessel when that space is itself constrained.

WFI2 

DETERMINATION OF ENZYME-STEROID BINDING SITES 

BY CPMAS 13C NMRAND SELECTIVE EXCITATION 

Vincent Bork* and Jacob Schaefer 

Department of Chemistry, Washington University 

St. Louis, MO 63130 

Richard J. Auchus and Douglas F. Covey 

Department of Pharmacology, Washington University 

School of Medicine, St. Louis, MO 63110 

The spatial proximity of inequivalent 13C nuclei in solids, 

which have been multiply labeled with 13C, can be obtained from 

spin transfer rates in CPMAS experiments involving selective 

excitation. The selective excitation is used to invert just one 

line in the spectrum which arises from a particular 13C label. 

By varying a dipolar evolution time, 13C-13C connectivity is 

revealed by new peaks in the spectrum obtained as a difference 

between the normal CPMAS spectrum, and the CPMAS spectrum with 

selective excitation. Confusing natural-abundance background 

peaks disappear in the difference spectrum. This difference 

technique can be used to identify 13C-labeled chemical bonds in 

complex biological solids. For example, the technique has 

demonstrated that the insoluble adduct between a [13C2]- 

acetylenic steroid and human estradioldehydrogenase involves 

binding of the drug to both lysine and cystine residues.

WF14 

THE USE OF MULTIPLE ECHO ACQUISITION AND STIMULATED ECHO5 

TO DETECT SLOW MOTIONS 

S. D. Kennedy, S. Ganapathy, S. Swanson, R. 8. Bryant 

Department of Biophysics 

University of Rochester Medical Center 

Rochester, New York 14642 

The use of Fourier transformed echo trains was described by 

Zilm at the ENC last year. The advantages for a number of 

studies include increases in signal to noise, clear 

demonstration of heterogeneous broadening, transverse 

relaxation time measurements rapidly, as well as sensitivity 

to motions of the spins various types. We have demonstrated 

that the method provides a very efficient monitor of ms 

motions in polymers. The techniques are equally well suited 

to the study of chemical exchange in the solid or spin 

exchanges caused by relaxation. In the basic spin echo train 

e~:periment, the time scale limitation i~ imposed by the 

effective transverse relaxation times in the system~ which 

may vary considerably from sample to sample, but are 

typically in the tens of ms range. 

The basic e~periment may be e~:tended in time by using a 

stimulated echo. The spins are phase encoded during the 

period ÷ollowing the 90 degree pulse or magnetization cycle 

by Hartmann-Hahn contact for example, then stored along z for 

a variable time during which motion or a magnetic or chemical 

exchange event may change the Larmor frequency. The read-out 

is accomplished with a third 90 degree pulse and the 

formation of a stimulated echo. This experiment extends the 

time scale of the motion observation to the carbon T, rather 

than the T2. We have applied this technique in a series of 

polymers to detect slow motions. In molecules containing 

nitrogen such as peptides~ the "4N may complicate 

interpretation of the data in terms of motions alone. The 

e~:periment, when combined with other rela~:ation time 

measurements and MASS~ provides an easy method for measuring 

the "4N T~, a parameter of interest in its own right. We 

report results on a series of amino acids and peptides that 

demonstrates the method and indicates the importance of 

nitrogen relaxation times in dynamical intrepretations.

WF16 

CHARACTERIZATION OF TRANSITION METAL SILICIDES 

WITH 2°Si NM:R SPECTROSCOPY 

T. M. Duncan* and D. M. Simonsen 1 


Murray Hill, NJ 07974. 

The ~Si NMR spectra of 26 silicides of transition metals (Ti, Zr, Hf, V, 

Nb, Ta, Cr, Mo, W, Mn, Fe, Ru, Co, Rh, N], Pd, Pt, and Cu) are reported. 

These metallic compounds which are used in semiconductor devices, exhibit 

NMR spectra with parameters ---10 times as large as those of organosilicon or 

silicon oxide compounds; 2%i isotropie shifts span the range from -1650 to 

-I-925 ppm, relative to TMS, and 2%i anisotropies extend to 325 ppm with 

most near 150 to 200 ppm. The isotropic shifts vary systematically with the 

Group of the metal atom, but are only weakly dependent on the Period; 

silicides of Group VIII metals with an even number of electrons (e.g. Fe, Ru, 

Ni, Pd, Pt) comprise the compounds with isotropic shifts greater than 1000 

ppm. Interpretation of the isotropic shifts will be presented. The shielding 

anisotropies are sensitive indicators of the bonding symmetry of the silicon 

site. In contrast to 13C anisotropies in which ~rs is almost exclusively 

downfield of all, 2%i anisotropies of metal silicides are well distributed 

between ~r 1 downfield and upfield of a I[. The relative position of o~ varies 

systematically with silicon site geometry, depending principally on the degree 

of bonding perpendicular and parallel to the axis of symmetry. Finally, 

silicides exist in several different stoichiometries for a given binary 

combination (e.g., TisSi3, TiSi, TiSi2). The large distribution of isotropic 

shifts and shielding anisotropies allows resolution of individual spectra and 

thus quantitative analysis of multiple phases in a inhomogeneous material 

I. Dep~rtrnent of Chemistry, Yale University, New Haven, Connecticut

WFlt 

HIGH-SPEED MAS IgF NMR OF FLUOROCARBON POLYMERS 

t 

Steven F. Dec, Robert A. Wind, and Gary E. Maciel 




A powerful tool for the elucidation of the microstructure of fluoro- 

carbon polymers is IgF NMR. Studies of this nature have previously been 

limited to the liquid state due, in part, to large homonuclear dipole- 

dipole interactions, which obscure any chemical shift fine structure that 

may be present in the NMR spectra of solid samples. In this poster we 

show that, by using a relatively simple magic-angle spinning system 

(rotational frequencies > 20 kHz), high-resolution solid-state 19F spec- 

tra can be obtained at high fields. Results for a number of polymers at 

rotational frequencies greater than 18 kHz show that sufficient resolu- 

tion is obtained at these spinning speeds to I) identify all major fluor- 

ine sites in the polymers (i.e., small chemical shift differences for a 

particular fluorine group, due to nearest neighbor effects, are readily 

measured); 2) permit a deconvolution of overlapping peaks to obtain the 

number of fluorine atoms occupying each site; and 3) determine the rela- 

tive amounts of each different monomer present. 

next-nearest neighbor effects in these systems is presented. 

19F NMR evidence of

WF20 

DESIGN OF AN EFFICIENT PROBE FOR HIGH FIELD 

MULTINUCLEAR CP/MAS NMR OF SOLIDS 

Preben Daugaard, Vagn Langer, and Hans O. Oakobsen* 

Department of Chemistry, University of Aarhus, 

DK-8000 Arhus C, Denmark 

Very high-speed, stable spinning is a desirable technique in multi- 

nuclear CP/MAS, MA5, or VAS (variable angle spinning) experiments of solid 

materials for several reasons. For example this applies to both high-field 

CP/MAS studies of spin-l/2 (e.g. 13C, ]SN, 31p, and ]]3Cd) and quadrupolar 

nuclei (e.g. liB, 2~Na, and 27AI). 

We describe the design of a high speed multinuclear CP/MAS probe for 

the 51 mm bore superconducting magnet of our Varian XL-300 spectrometer. 

The spinning speed of the 7 mm o.d. rotors can routinely and accurately be 

set at any value up to at least 10 kHz with a stability of a few hertz. 

Air drive pressures of I and 4 bar are required for 4.5 and 9.0 kHz spin- 

ning, respectively, lhe spinner assembly employs a separate double air 

bearing which acquires an air pressure of only i-2 bar for a11 spinning 

speeds up to 10 kHz. We also expect to be able to discuss preliminary re- 

sults for the design of a 15 kHz spinner assembly during the meeting. 

The simplicity of the splnner assembly, and the high sensitivity and 

high electronic efficiency of the probe wili be demonstrated along with 

"real life" applications. 

0

WF22 

ORIENTATION OF THE 15N CHEMICAL SHIFT TENSOR 

IN A POLYCRYSTALLINE DIPEPTIDE 

C.J. HartF.ell., T.K. Pratum and G.P. Drobny 

Department o/Chemistr!t, Universitlj o/ Washington, Seattle, WA. 98195 

ABSTRACT 

In an effort to circumvent the ambiguities inherent in a determination of the 

orientation of a chemical shift tensor in the molecular frame of a polycD'stalline solid: 

we have pursued a study of the mutual orientation of three tensor interactions. In 

this study of polycrystalline L-[1-13Ci - alanyl-lilSN ~-alanine we have oriented the lSN 

chemical shift tensor in the molecul~ frame by reference to two dipole interactions. 

The 13C-ISN and lSN-H dipole interactions axe probed using a modification of the 

experiment of Stoll, Vega and Vaughan. The I H dipole-modulated 13C dipole-coupled 

lSlN spectrum is obtained as a transform of the data in t2. 

From simulations of the experimental spectra, two sets of polar angles are de- 

termined relating the 13C-lSN and lSN-H dipoles to the IsN chemical shift tensor. 

We have determined refined values for the polar angles Bc~ and c~c~ describing the 

orientation of the 13c-lsN bond to the tensor. The angle ~3cx describing the angle 

between 033 and the 13C- lSN bond is 106 = and the angle ac.~ describing rotation 

about 033 is 5 c. The angle ~3~H is 19 =. This experiment verifies the results of the 

13C dipole-coupled aSN powder spectra and simulations showing that or3 lies in the 

peptide plane and o~2 is nearly perpendicular to the plane.

WF24 

VT CP/MAS NMR OF ANTIFERROMAGNETIC METAL COMPLEXES 

Gordon. C__~. Campbell and James F. Haw 

Department of Chemistry, Texas A&M University 

College Station, TX 77843 

Drawing on our previous experience with variable-temperature (FT) CP/MAS 

NMR of paramagnetic species 1,2, we are now applying the technique to the study of 

antiferromagnetic materials. Antiferromagnetism is found in a wide variety of 

transition metal dimers and complexes in which a low-lying triplet excited 

electronic energy state lies above a singlet ground state. Spin pairing in the 

singlet state at low temperatures leads to diamagnetism, while at higher 

temperatures the triplet state is significantly populated, and these substances 

exhibit the properties of paramagnetic materials. 

It is thus difficult in many cases to observe CP/MAS NMR spectra of anti- 

ferromagnetic solids at or above room temperature. Lowering the sample temp- 

erature is found to significantly increase the amount of information available 

from CP/MAS NMR data. Not only do resonances closer to metal centers become 

observable, but the temperature dependence 

of the chemical shifts may give quant- 

itative information about the electronic 

character of the species. A good example 

of this is afforded by the 13C CP/MAS NMR 

data for copper(ll) n-butyrate hydrate 

dimer presented in the figure, where mag- 

netically inequivalent sites (eg., CI and 

CI') are also observable. 

1. J. F. Haw and G. C. Campbell, 

J__~. Ma~n. Reson., 66, 558 (1986). 

VARIABLE TEPdPE]u.,tTURE C-13 CP/IdAS SPECTRA 

OF COPPlg:I {11) N-BUTYRATE HYDRATE DIMER 

¢~ ~K 

2. G. C. Campbell, R. C. Crosby, and J. F. Haw, 

J. Ma~n. Reson. 69 191 (1986). I 1 i

WF26 

TEMPERATUREVARIABLE SOLID SOLUTION CPMAS NMR STUDIES 

OF DYES IN GLASSY POLYMERS 

Bernd Wehrle and Plans-Heinrich Limbach* 

Institut ffir Physikalische Chemie der Universitit Freiburg l.Br., 

Albertstr.21, 7800 Freiburg, West Germany 

Photoreactive solids such as dyes imbedded in solid tnatrices are of 

considerable technical and theoretical interest. We report here the use of 

temperature variable CPMAS NMR spectroscopy for the study of structure 

and dynamics of dyes dissolved in glassy polymers. As in liquid solution 

state NMR, solution state NMR studies are greatly aided if matrix signals 

are absent in the spectra. Since most of the known organic dyes but few 

polymers contain nitrogen we propose here I~N CPMAS NMR of I~N en- 

riched dyes. This method has also the advantage that spectra can be re- 

corded even at fairly low dye concentrations. Thus, interesting lnfor- 

mations about the structure and the dynamics of dyes in solid matrices 

can be obtained, such as fast chemical reactions inside the dye, rotational 

and transverse diffusion, or slow crystallization. 

In particular, we present here low temperature I~,N CPMAS NMR spectra 

of a tetraazaannulene derivative (TTAA) dissolved to a few percent in 

glassy polystyrene, PMMA, etc. In crystalline TTAA fasl proton tau~o- 

merism leads to sharp I~N NMR lines whith temperature dependent positi- 

ons. ~ By contrast, the solid solution ~N NMR lines of TTAA in glassy po- 

lymers are broad but show a characteristic temperature dependence. 2D 

experiments reveal that this broadening is inhomogeneous. The lineshapes 

can be simulated with the assumption of a broad gaussian distribution of 

different sites in the glass in which dye molecules experience a differenl 

reaction profile of tautomerism. Within the NMR timescale the molecu]es do 

not rotate nor are able to exchange sites at room temperature. Thus, dye 

tautomerism can be used as a novel probe for local order. Some conse- 

quences of for the understandung of chemical reactions in condensed 

matter are discussed. 

1. H.H.Limbach, B.Wehrle, H.Zimmermann, R.D.Kendrick, C.S.Yannoni 

j.Am.Chem.Soc., in press).

WF28 

DYNAMIC NUCLEAR POLARIZATION IN ORGANIC CONDUCTORS 

t 

Robert A. Wind, Herman Lock and Gary E. Maciel 




In solids containing unpaired electrons, nuclear spin magnetization 

can be enhanced via Dynamic Nuclear Polarization (DNP). This can be used 

for, among other things, increasing the signal-to-noise ratio of an NMR 

signal, obtaining information about the vicinity of the unpaired elec- 

trons and determination of electron mobilities. We have applied DNP in 

combination with IH and 13C NMR to two organic compounds that become 

metallic by doping them with a suitable agent, namely trans-polyacetylene 

and (fluoroanthenyl)2PF 6. The main results are: 

(i) Trans-polyacetylene. Even undoped trans-polyacetylene contains 

mobile electrons, the so-called "solitons". We found that electron 

mobility is restricted: part of the time the unpaired electrons can be 

considered as fixed in space, whereas the rest of the time they are 

moving over the polymer chains with about the velocity of sound. Fur- 

thermore, the influence of air oxidation has been investigated, the 

effects both on the amount and types of defects created by this oxidation 

and on the amount and mobility of the unpaired electrons. 

(ii) (Fluoranthenyl)2PF6. This work has been done in collaboration 

with Michael Mehring. The 13 C spectrum consists of seven distinguishable 

lines. It has been found that the locations of at least four of these 

lines shift by irradiating with increasing microwave power at the ESR 

frequency. This proves that these locations are at least partially 

determined by a Knight shift due to the mobile electrons.

WF30 

SOLID STATE ~P MAS NMR AS A TOOL FOR STUDYING 3-DIMENSIONAL 

SOLIDS: THE CHALCOPYRITES ZnSiPe, ZnSnPe, ZnGePe, AND 

RELATED MATERIALS 

Robin A. Nissan', and T. A. Hewston 

Naval Weapons Center, China Lake, CA 93555 

Three-dimensional solids containing phosphorus in a 

reduced state are of interest as tough, stable ceramic mat- 

erials. These materials may be synthesized from their con- 

stituent elements or from combinations of binary materials at 

elevated temperatures. Phase purity and structural integrity 

are generally monitored by X-ray powder diffraction. 

Elemental analysis by wet chemical methods or by electron 

microscopy yields information on stoichiometry. Structure 

determinations for new materials require single crystal X-ray 

diffraction analyses. Phase-impure materials are difficult 

to analyze by these techniques, especially if the materials 

include amorphous phases which would be transparent to X-rays 

and complicate elemental analyses. New methods for the ana- 

lysis of 3-dimensional solids are required. 

We have initiated a program to study inorganic phos- 

phides by solid state ~P MAS NMR. The chalcopyrites 

ZnSiP~,, ZnGePe, and ZnSnPe have the ordered zincblende 

structure. This family of materials was chosen for our 

initial studies since a series of isostructural compounds 

existed where one atom could be varied. In addition, we have 

studied a series of binary phosphides including Mg-,P;., GaP, 

and CaP. The most striking result here is the spectral 

simplicity. Chemical shift anisotropy and dipole-dipole 

broadening pose no problems at 81 MHz in most cases. The 

lines are sharp and crystallographically unique phosphorus 

sites are distinguished- One notable exception is ZrP where 

we observe two overlapping axially symmetric powder patterns 

representing the two crystallographic sites of phosphorus in 

this compound. Results will also be presented for CdPS::~ 

where the Pe units occupy cation sites. Studies of relaxa- 

tion times and quantitative analysis of mixtures are 

presently under way.

WF32 

SOLID STATE NMR OF PROTEINS 

P. Stewart, R. McNamara, D. Chen, C. Lee, D. White, and S. Opella 



Philadelphia, Pennsylvania 19104 

Recent results from solid state NMR studies of unoriented and oriented 

protein samples will be presented. The analysis of powder pattern 

lineshapes and relaxation parameters as a function of temperature is being 

used to describe backbone and sidechain dynamics of proteins. A number 

of different spectral parameters measured in oriented samples are being 

interpreted in terms of structural parameters. In particular, a general 

method for determining the mutual orientations of adjacent peptide planes 

from solid state NMR measurements is being developed. 

The spectroscopic experiments involve the observation of 13C, 15N and 

14N resonances so that chemical shift, quadrupole, and dipole-dipole 

interactions can be examined in multiple sites. The samples include 

lysozyme, filamentous bacteriophage coat protein, and model peptides.

WF34 

13C MAS NMR STUDIES OF VARIOUS 

SUPPORTED METAL CATALYSTS 

°D.M.Simonsena, K.W.Zilm a, T.Root b, T.M.Duncanc, L.Bonneviotd, and G.Hallere 

aDept, of Chemistry, Yale University, New Haven, CT 06511 

The structure of small molecules chemisorbed on supported metal 

catalyst systems has been extensively studied by broad-line NMR. To date, 

relatively little work has been done on these systems with magic-angle spinning 

(MAS) techniques. Previous studies, especially those on supported Pt catalysts, 

have indicated that MAS NMR experiments may be of limited utility in 

characterizing chemisorbed species on surfaces due to problems with Knight 

shifts and sample inhomogeneity. This poster will present both static powder 

patterns and MAS spectra of 13C-labelled ethylene chemisorbed on platinum and 

palladium catalysts as well as 13CO chemisorbed on platinum, palladium, 

ruthenium, and rhodium catalysts. As expected 13C MAS NMR spectra show no 

significant line narrowing for the 13CO/Pt system. However, MAS techniques 

allow the resolution of relatively narrow individual peaks in all other samples 

studied. By using both F'I" and CP methods with MAS reaction chemistry can be 

followed in these systems under controlled conditions. The effects of magnetic 

susceptibilities and Knight shifts on these spectra will also be discussed. 

bDept, of Chemical Engineering, UW-Madison, Madison, Wl 

CA T & T Bell Laboratories, Murray Hill, NJ 

dUniversite P. et M. Curie, Paris, France 

eDept, of Chemical Engineering, Yale University, New Haven, CT

WF36 

A PROTON MAS NMR METHOD FOR DETERMINING INTIMATE MIXING IN POLYMER BLENDS 

D.L. VanderHart" and W.F. Manders, National Bureau of Standards, Gaithersburg, 

MD 20899, and R.S. Stein and W. Hermans, Polymer Science and Engineering 

Department, University of Massachusetts, Amhearst, MA 01002 

Intimate mixing (on a scale less than i nm) in polymers can be probed 

effectively by laC CP-MAS techniques as has been shown by Schaefer, et al. 

(Macromolecules, 1981, 14, 188). The basic idea is that if one mixes 

deuterated and protonated polymers, cross polarization (CP) signals from the 

carbons on the deuterated polymers will arise only if dipolar-coupled protons 

are close by, say, 0.5 nm or less. A non-trivial problem in this method, 

however, is that perdeuterated polymers usually contain 1 - 2% residual 

protons, and these 'Impurity' protons, as well as protons on the prononated 

chains, generate deuterated carbon signals. 

In this poster, we show that similar information is available by observing 

the impurity protons directly. The impurity protons are different from the 

protons on the protonated chains since their average interaction with other 

protons is much weaker. In a relatively rigid polymer, at low magic angle 

spinning (](AS) frequencies, the impurity proton signals in the deuterated 

homopolymer will be broken up into well-defined sidebands and centerbands (see 

spectra A and B, non-spinning and 2.2kHz spinning, respectively, of deuterated 

atactic polystyrene (aPS)). In contrast, a relatively rigid protonated 

homopolymer will produce no narrow centerbands or sidebands because of the 

stronger proton dipolar interactions and the concurrent fast spin-exchange 

behavior. In a mixture of relatively rigid polymers, one deuterated and the 

other protonated, there will be an attenuation of the narrowed centerband and 

sidebands from the impurity protons when mixing is intimate, i.e. when protons 

from the protonated polymer lie within, say, 0.8 nm of the impurity protons. 

Spectrum C is that of a protonated aPS mixed with the deuterated aPS using 2.2 

kHz spinning and a spectral display where the impurity protons contribute 

equal signals to those in B. An 85% attenuation, compared to B, of the 

aromatic proton centerband at 7 ppm is seen in the blend spectrum. As 

expected in this blend of similar polymers with similar tacticities, mixing is 

quite intimate. Interference from the broad and strong protonated aPS 

resonances is limited to a rolling baseline. Because of M.AS, and the 

resonance distinctions which ensue, this 

A analysis can be carried out in the presence 

of varying amounts of mobile solvent residues 

which, in our case, contribute to the 

aliphatic bands between 0 and 3 ppm. This 

technique offers an important sensitivity 

advantage over the 13C CP technique. The 

requirement for two relatively rigid polymers 

is common to both techniques, so low 

temperature operation is sometimes mandated. 

Perhaps the best news is that this technique 

represents a minor comeback for the 

beleaguered single-pulse ID experiment. 

Bandwidth requirements should allow one to 

carry out this experiment using high- 

resolution electronics. 

I I I I I I I l I 

40 20 0 -20 PPM

• WF38 

29SI DYNAMIC NUCLEAR POLARIZATION STUDIES OF 

DEHYDROGENATED AMORPHOUS SILICON 

H. Lock m, G. E. Maciel, R. A. Wind 

Department of Chemistry, Colorado State University 

and 

N. Zumbulyadis 

Corporate Research Laboratories 

Eastman Kodak Co., Rochester, New York 14650 

Dehydrogenated amorphous silicon, a-Si, contains a large number of 

dangllng-bond paramagnetlc centers. This opens the possibility of 

performing 29Si dynamic nuclear polarization (DNP) experiments, 

where the 29SI polarization is enhanced by irradiating at or near 

the electron larmor frequency. We performed 29Si DNP in a-Si 

in an external magnetic field of 1.4 T, corresponding to 29Si 

larmor frequency of 11.9 MHz, and an electron larmor frequency, 

re, of ca. 40 GHz. The amplitude of the microwave field, B 1, was 

0.06 mT (max.). 

The main results are: 

I. The 29Si DNP enhancement is antisymmetrical around re, 

indicating that the dangling bonds are fixed in space. 

2. The shape of the DNP enhancement curve as a function of 

microwave frequency offset is independent of BI. This means that 

at 40 GHz the ESR llne is mainly inhomogeneously broadened, which 

is confirmed by ESR measurements at 9 and 40 GHz. 

3. For a B1 of 0.06 mT the maximum 29Si DNP enhancement is 40. 

This value is obtained using a microwave frequency ±29 MHz away 

from the electron larmor frequency. The enhancement is probably 

due to an unresolved solid state effect. 

4. The integrated intensity of the 29Si spectrum, enhanced vi____aa 

DNP is the same with and without magic angle spinning. Hence, the 

DNP effect is mainly due to direct interactions between the 29Si 

nuclei and the unpaired electrons.

WF40 

NONAXIALLT SYMMETRIC DIPOLAR COUPLINGS IN SOLIDS AND LIQUID CRYSTALS 

m 

T.P. Jarvie, A.M. Thayer, a J.M. Mlllar m 

, M. Luzar and A. Pines 


Small amplitude motions in solids can induce an asymmetry in the 

dipolar coupling of two spln I=I/2 nuclei. In contrast to hlgh-field 

NMR, such subtle motlonal effects are readily observed in the zero field 

NMR spectrum. Experimental examples can be found in the llbratlonal 

motions of the water molecules In a polyerystalllne hydrate, the proton 

Jumps In a hydrogen-bonded carboxyllc acid dimer, and the diffusive Jumps 

of a probe molecule in an unaligned blaxlal smectlc E liquid crystal 

phase. An interesting experimental result shows that the presence of a 

nonzero asymmetry parameter in the dlpolar coupling produces a quenching 

effect of the coupling to small residual or local fields in analogy to a 

spin I=I system (I) in zero field. 

I. G.W. Leppelmeler and E.L. Harm, Phys. Rev. Iqi, 72~ (1966).

WF42 

ERRORS IN MAPPING RF MAGNETIC FIELDS 

Robert G. Bryant, Jerzy Szumowski, + and Joseph P. Hornak 

Biophysics Department 

University of Rochester 

Rochester, NY 14642 

÷ Radiology Department 

University of Rochester Medical Center 


* Chemistry Department 

Rochester Institute of Technology 


Homogeneous radio frequency magnetic flelds are necessary for the 

production of uniform contrast nuclear magnetic resonance images and for 

spatlally locallzed spectroscopy, it is often tempting to map the RF 

magnetic flelds of a resonator from the image intensity of a water 

phantom placed within the resonator. The resultant field maps are 

highly dependent on the pulse sequence used to produce the phantom 

images, and not always equlvalent. RF magnetic fleld maps obtained 

using a pickup toll probe moved about the resonator and spin echo and 

GRASS imaging sequences on a GE Signa Imager will be presented for 

comparison. The basis for large observed differences betveen the 

techniques are discussed. 

4~

WF44 

PROTON DETECTED SIP-IH HETCOR OF DNA FRAGMENTS 

Robert Santini* 

Claude R. Jones 

David Gorenstein 


Purdue University 

West Lafayette, IN 47907 

Many spectrometers can be converted to simultaneous broad band operation 

of both the transmit-receive and decoupler channels. With some extra equipment 

(an additional broad band board, a PTS 160, filters, and a 10 watt amplifier) the 

conversion of an XL-200A back and forth between a dual broad band configuration 

and a standard configuration suitable for use in a multiuser environment can be 

accomplished with a few cable changes. Proton detected sIp-~H HETCOR spectra 

off synthetic DNA fragments with up to 14 base pairs were obtained in a dual 

broad band mode using a standard 5rnm probe. The proton transitions were first 

saturated (1) and a constant time sequence (2) was used. The pulse sequence 

was phase cycled to give a pure absorption phase spectrum after a hypercomplex 

transform. 

1. V. Sklenar, H. Miyashiro, G. Zon, H.T. Miles, and A. Bax, 

FEBS Letters (1986), 208, 94 

2. H. Kessler, C. Griensinger, J. Zarbock, and H.R. Loosli, J. 

Magn. Reson. (1984), 57, 331

WF46 

DEUTERIUM NMR STUDY OF METHYL GROUP DYNAMICS 

IN L-ALANINE 

Kebede Beshah*, Bdvard T. OleJniczak +, and Robert G. Griffin 

Francis Bitter National Nagnet Laboratory 


Cambridge, NA 02139 

Deuterium quadrupole echo spectroscopy is used to study the 

dynamics of the CD 3 group in polycrystalline L-alanine-d 3. Temperature- 

dependent quadrupole echo lineshapes, their spectral intensities and x- 

dependence, and the anisotropy of the 2H spln-lattice relaxatlon were 

employed to determine the rate and mechanism of the -CD 3 group motion. 

The rigid lattice Pake pattern observed at low temperature (T < -120°C) 

transforms to a triplet spectrum characteristic of threefold Jumps in the 

intermediate exchange regime (-120°C to -70°C) and this in turn to a 

Pake pattern of reduced breadth at higher temperatures (T > -70°C). The 

quadrupole echo lineshapes and their x-dependence, which are especially 

sensitive to the rate and mechanism of the motion, can be simulated 

quantitatively vith the threefold jump model. Ve find ga = 20.0 kJlmole 

for this process vhich is higher than is observed for most methyl groups, 

probably because of steric crowding in the L-bla molecule. Finally, we 

observe a lineshape due to the presence of multiple crystallographic 

forms which suggest that this technique can be extended to studies of the 

dynamics of more complex systems. 

+Present address: Abbott Laboratories 

North Chicago, IL 60046

WF4S 

SEGMENTAL DYNAMICS IN NYLON 66 BY DEUTERIUM NMR 

Hitoshi Miura* and Alan D. English 

Central Research and Development Department 

Experimental Station 

E. I. Dupont de Nemours & Company 

Wilmington, Delaware 19898 

The study of chain dynamics of nylon 66 by deuterium 

NMR is described. We prepared five selectively deuterated 

samples of nylon 66, for which T1 data and quadrupolar echo 

powder spectra were obtained at various temperatures from 

-I19C to 228C. By using the difference of T1 in the 

different phases, we can separate their spectra from each 

other. This enables us to study the chain dynamics of each 

phase independently. 

The motion at different places in the methylene 

segments in nylon 66 are quite different and are strongly 

dependent upon temperature. Line shape calculations for 

several kinds of models of molecular motion are compared to 

experimental spectra, which give important information on 

the segmental motion of the polymer at various temperatures. 

Models of motion in "pinned segments" composed of either 

four or six methylene segments in either crystalline or 

noncrystalline domains may be examined with this system. We 

will present the results and discuss them.

WF50 

Solid State NMR Dynamics Studies of Duplex RNA 

Pearl Tsang*, Robert L. Void and Regitze R. Void 

Department of Chemistry B-014 

University of California at San Diego 

La Jolla, CA. 92093 

The results of dynamic studies of duplex RNA, obtained through a combination of 

solid state H-2 and P-31 NMR techniques, are presented in this poster. The base pair and 

phosphodiester backbone motions of duplexes at various relative humidities have been 

separately examined using deuterium NMR to study purine-8 deuterated sites and phos- 

phorous NMR to study the phosphodiester backbone, respectively. Deuterium spin-lattice 

relaxation rates of RNA are determined both at 38.4 and 76.8 MHz. P-31 NMR lineshape 

studies of RNA duplexes are also conducted. 

Deuterium spin-lattice relaxation rates for the various purine-8 sites of the RNA du- 

plexes studied show a trend of steadily decreasing T1 with increasing relative humidity. 

Based upon the field dependence of the RNA T1 values, it appears that collective torsional 

modes may be a dominant factor in the relaxation process. 

The results obtained for RNA are briefly compared to those obtained from analo- 

gous DNA samples. Significant dynamic differences between DNA and RNA have been 

observed, based upon the rather different spin-lattice relaxation rates obtained for the two 

species. P-31 NMR results for the RNA are also compared to those of the DNA.

WF52 

ANALYSIS OF CONPLBX NIXTURES BY ULTRAHIGH RESOLUTION NNR 

Steven R. Naple and Adam Allerhand 

Department of Chemistry, Indiana University, Bloomington, IN 47405 

Ultra-high resolution NNR methodology has increased the ability of the 

NNR spectroscopist to observe minor component peaks of complex mixtures 

without the use of "solvent" suppression techniques. It is now possible to 

detect minor peaks in the presence of laJor peaks which are 10 a times 

larger. Results from the following examples will be discussed: (1) The 

observation and kinetics of the aldo] condensation dimer of acetone. 

(2) The assignment of individual components in a complex petroleum fraction. 

(3) The determination of the equilibrium anomerlc composition of 

carbohydrate solutions. These examples cover line widths ranging from very 

narrow to those typically encountered in 13C NNR of simple and complex 

organic molecules. We will also present information about the 

Identification of instrumental artifacts and the demands placed upon the 

computer, both in the horizontal (number of data points or words) and 

vertical (number of bits per word) directions, by ultra-high resolution NHR 

methodology.


2D EXCHANGE NMR IN NON-SPINNING POWDERS 

C. Schmidt~ S. Kaufmann~ S. Wefing~ D. Theimer, 

B. Bl~mich" and H. W. Spiess~ 

Max-Planck-Institut f~r Polymerforschung~ 

Postfach 3148, D-6500 Mainz 

Information about molecular motions in isotropic 

solids is typically derived from lineshape analyses of 

wideline NMR spectra~ Nhile in liquid samples 2D exchange 

NMR has become an accepted method. In 2D exchange spectra 

some of the information hidden in the lineshapes of 1D 

spectra is reencoded into frequency coordinates of 

exchange signals, where it is accessible more accurately 

and in a model-independent fashion. 

We have studied deuteron and C-13 2D exchange NMR 

for the characterization of molecular motions in powders 

and amorphous solid samples. The deuteron quadrupole 

coupling tensor is axially symmetric, so that particu- 

larly simple exchange signals result. Discrete jumps are 

characterized by elliptical exchange singularities, where 

the excentricity of the ellipse is a direct measure of 

the jump angle. Diffusive motions result in homogeneous 

broadening with.characteristic 2D lineshapes discrimina- 

ting different stages of partial diffusion towards the 

full diffusion limit. For short mixing times pure 

diffusion~ diffusion in connection with discrete jumps, 

and pure jump motions can be distinguished. 

The 2D exchange experiment can also be performed in 

C-13 NMR on selectively labelled compounds. The asymmetry 

of the chemical shielding tensor, however~ leads to more 

complicated 2D exchange patterns. Experimental and theo- 

retical data demonstrate that the wideline 2D exchange 

experiment produces a direct image of the jump angle 

distribution. 

Ref erences: 

1) C. Schmidt, S. Wefing~ B. Bl~mich and H.'W. Spiess, 

Chem. Phys. Lett. 130, 84 (198b). 

2) M. Linder, A. Hbhener and R. R. Ernst~ J. Chem. Phys. 

73, 4959 ~1980).

WF56 

LOCALIZED PROTON DENSITY. RELAXATION TIMES AND SELF DIFFUSION 

COEFFICIENT MEASUREMENTS IN SINGLE CELLS BY NMR MICROSCOPY. 

J. AEuayo, S. Blackband, J. Schoenlger and M. Mattlngly*, Division 

of NMR Research, Johns Hopkins University Medical School, Baltlmore, 

Maryland 21205. 

l~urDose. To obtain and intrepret localised measurements of proton 

density, relaxation times (T1/T2, and self diffusion coefficients of 

regions within a single cell. 

Methods. A modified Bruker AM 400 spectrometer has been equipped 

with imaging software and hardware accessories. Using a 50 mm set 

of gradient coils up to 20 G/cm have been generated during imaging 

experiments. In order to optimize sensitivity, a 5 mm solenoid were 

used for these studies. A spin echo pulse sequence was used to 

obtain proton density weighted images. Multi-echo and inversion 

recovery programs were used to obtain T 2 and T 1 weighted images 

respectively. To obtain self diffusion measurements, the spin echo 

and multi-echo programs were modified by adding two pulsed gradients 

on either side of the refocusing 180 ° pulse. In these programs a 

selective 90 ° pulse was used. Ova were obtained from Xenopus 

laevius. 

Results. The highest resolution to date has been I0 X 13 X 250 

microns (I). A homogeneous cell nucleus and heterogenous cytoplasm 

were observed. The highest proton density was in the cell nucleus 

followed by the marginal zone (region around the nucleus) and 

finally the cytoplasm. The cytoplasm has a high lipid content as 

evidenced by a chemically shifted component of the signal from this 

region. The cell nuclues was noted to have a long T 1 that was 

similar to the T 1 of the surrounding buffer solution and longer than 

that of the cytoplasm. The T 2 of the nucleus was longer than that 

of the cytoplasm. Diffusion studies are in the process of being 

Intrepreted but indicate that the water in the cell nucleus is 

similiar to that of free water. 

Conclusion. It is now possible to obtain images of single cells and 

to obtain localized TI, T2, proton density and self diffusion 

measurements from within different regions of single cells. The 

properties of the cell nucleus in the cell system that we chose to 

study were significantly different than those of the surrounding 

cytoplasm. Further study and correlation between these results and 

previous observation by other techniques is important in order to 

understand the meaning of these observations. 

I. Aguayo J.B., Blackband S.J., Schoeniger J.S., Mattingly M.O., and 

Hintermann M., Nature, 322, 190-192, 1986.

WF58 

SPATIAL LOCALISATION OF ~lp ~LR SPECTROSCOPY USING PHASE 

MODULATED ROTATING FRAI~E IMAGING. 

Kartin J. Blackledse*, Peter Styles and Georse K. Radda 

X.R.C. CLINICAL NAGNETIC RESONANCE FACILITY, JOHN RADCLIFFE HOSPITAL, 

OXFORD ENGLAND U.K. 

Rotating frame imaging (R.F.I.) using the B, field gradient of a 

surface coil has been shown to be a viable method for localislng 

phosphorus spectra in-vivo. Use of separate coils for transmitting and 

receivin E signal ensures that the encoding field gradient is linear and 

the shape of this field throughout the interrogated resion is flat and 

planar. As normally implemented, R.F.I. is an inherently inefficient 

technique; this is because the observation pulse is incremented, and 

received signal is amplitude modulated with respect to incremental 

pulse ansle. The magnetisatlon precesses about the x-axis of the 

rotatin 5 frame_, so that of the two components (y and z), only the y 

component is detected. To overcome this insensitivity, it i$ necessary 

to detect the z component. This is achieved by 'flipping' the 

masnetisation, immediately after the incremental pulse, into the x-y 

plane usin 5 a 7/2 pulse applied alon E the y axis This signal is phase 

modulated, the relative x and y component masnetisation in the rotatin$ 

frame varies with pulse angle. For this modulation to be useful, the 

phase encoding pulse (p.e.p) is required to have a bandwidth in both 

B, and Bo over which it is effective in accurately transposln8 the 

phase of the mnsnetisation vector from the y-z to the x-y plane. 

Usin 5 a double coil (with smaller receiver coil) we receive from the 

region (.2-.8) radii of the transmitter coil away from the surface. In 

this resion, the B, field strength varies from >.5 to

WF60 

SENSITIVITY OF SURFACE COILS TO DEEP LYING VOLUMES 

William J. Tboma , ~ichael J. Albright ~, 

Piotr M. Starewicz" and Truman R. Brown 

Fo~Chase Cancer Center, Philadelphia, PA 19111 

Siemens Medical Systems, Iselin, NJ 08830 

Ne have acquired rith an 8.5 cm-single turn3[urface coil in a 1M bore 

magnet operating at 1.5 T a single acquisition P spectrum (26 MHz) of the 

human calf that clearly displays ATP J-coupling and has a pbosphocreatine 

signal to noise of 25 with a 7 hertz gaussian filter. Obviously, this is 

adequate sensitivity for the entire volume. Unfortunately, in many cases, in 

order to distinquish amoung various physiological responses, it is required 

that the volume selected for observation be restricted. As the volume from 

which the signal is derived becomes smaller the sensitivity of the detection 

coil becomes critical. It is well known that the most important factors in 

coil sensitivity are the distance from the coil to the volume from which the 

signal originates, and the Q of the coil. Other factors that are important 

include the geometric shape of the coil, number of turns, and shielding of the 

coil from dielectric losses. 

We have undertaken a study of the sensitivity of surface coils for small 

regions as a function of their depth for various surface coil designs, 

different turn numbers, various faraday shields, coil radius as a function of 

sample volume size, and coil Q. The Q of the coil was measured by determining 

the 90 ° pulse at, and the resultant signal from, a 2 cm chamber containing 

phenylphosphonate in the center of the coil. Five and 10 cm thick phantoms 

of dimensions large compared to the surface coil diameter were filled with 

solutions of differing ionic strength and placed between the coils and a 2S ml 

spherical sample. 

The resultant sensitivity of the various coils rill be reported as a 

function of the above parameters.

WF62 

CONVOLUTION CHEMICAL SHIFT IMAGING 

M.D. COCKMAN- (a,b) and T.H. MARECI (b,c) 

Departments of (a)Chemistry, (b)Radiology, and (c)Physics 

University of Florida, Gainesville, FL 32610 

One of the challenges of NMR imaging is the simultaneous 

collection of spatial and chemical information. However, 

non-selectlve Fourier chemical shift imaging methods, in 

which spatial information is obtained for every chemical 

resonance in a spectrum, hmve been time-consuming and require 

at least a three-dlmensional Fourier transformation 

algorithm. By a straightforward modification of the method of 

Sepponen and coworkers (1), we have developed a new method of 

non-selectlve chemical shift imaging which requires less 

total data acquisition time and a simpler processing scheme. 

The new method is accomplished in part by requiring that 

the controlled inhomogeneity introduced by the gradients be 

smaller than the inherent inhomogeneity which gives rise to 

the chemical shift effect. The use of small gradient 

strengths has the benefit of increasing the S/N ratio of the 

resulting image. A second requirement of our method is that 

the magnitudes of a time delay, during which chemical shift 

encoding occurs, and a gradient, during which spatial 

encoding occurs, are changed in concert with each other. This 

simultaneous stepping has the effect of creating a modulation 

function whose Fourier transform is the convolution of a 

function of spatial position and a function of chemical shift 

frequency. Our technique has therefore been named 

aconvolution chemical shift imaging'. This imaging scheme 

introduces spectral information into all spatial imaging 

dimensions. Thus a three-dimensional chemical shift imaging 

experiment can be reduced to a two-dimensional convolution 

chemical shift imaging experiment which retains the same 

information. 

Convolution chemical shift imaging requires that the 

spatial field of view in frequency units must be on the order 

of or smaller than the chemical shift separation of interest 

if one wishes to resolve a spatial image from each chemical 

shift species. Therefore the method is best suited for small 

objects at high field. 

The convolution chemical shift imaging method has been 

implemented on a General Electric CSI-2 imager/spectrometer. 

Examples of the imaging of phantoms using the method are 

presented. 

This research was supported in part by the NIH Biotechnology 

Resource Grant (P41-RR-02278) and the Veterans Administration 

Medical Research Service. 

(1) R.E. Sepponen, J.T. Sipponen, and J.I. Tanttu, 

Assist. Tomogr. 8, 585 (1984). 

J. Comput.

WF64- POSTERS 

NMR FLOW IMAGING 

C. L. Dumoulln*, S. P. Souza, H. R. Hart Jr. 

General Electric Research and Development Center 

PO gox 8, Schenectady, New York 12301 

Many flow sensitive NMR procedures have been proposed and demonstrated. 

All of these methods rely on either longitudinal magnetization or transverse 

magnetization for flow discrimination. Time-of-flight and spin washout are 

examples of flow sensitive techniques which make use of longitudinal magneti- 

zation. In these methods, the longitudinal magnetization is changed in one 

location and monitored in another downstream from the first. Techniqdes which 

make use of transverse magnetization such as the one described below typically 

monitor the phase of spin magnetization and thus are not constrained by the 

geometry of flow. 

The most significant problem in blood flow imaging in animals or humans 

is the suppression of signals arising from non-moving spins. This is a par- 

ticularly severe problem because blood vessels are relatively small when com- 

pared to the volume of the surrounding tissue and blood flow is usually pulsa- 

tile rather than constant. The rapid-scan, phase contrast technique presented 

here circumvents these problems and has proven very useful in obtaining non- 

invasive angiograms of healthy and diseased patients. 

The flow-induced phase shift of a bi-polar gradient pulse is simply 

- vVTA G 

where ~ is the flow-induced phase shift, 7 is the gryomagnetic ratio, V is the 

component of spin velocity in the direction of the applied magnetic field gra- 

dient, T is the time between the centers of the lobes of the bipolar gradient 

and A G is the area of the first lobe in the bi-polar pulse (the area of the 

second lobe is -AG). To selectively detect flow in an imaging or spectroscopy 

procedure one can simply acquire two sets of data under different conditions 

of V, T or A G. We have found that the inversion of the bi-polar gradient 

pulse gives the best results. Thus, two echoes are obtained, one with 

- 7VTA C and the other with # - 7VT(-Ac). Moving spins are selectively 

detected ~ and stationary spins suppresse~ by taking the difference of the two 

echoes. Since the flow sensitivity of such a procedure is only in the direc- 

tion of the applied field gradient, two flow images are obtained with orthogo- 

nal flow sensitivities and combined to give the total flow image. The inten- 

sity of each pixel in the image is a quantitative measure of flow provided the 

flow-induced phase shift, ~, is less than about 1 radian. 

Suppression of non-moving spins can be enhanced by a weak dephasing gra- 

dient applied in the direction of the image projection. Such a gradient 

dephases spin magnetization over the large volume of non-moving spins and has 

little effect in the relatively small vessels. Additional suppression can be 

obtained by acquiring data very quickly and with short pulse-to-pulse inter- 

vals. Rapid scanning saturates non-moving spins while spins which move into 

the detection region are fully relaxed. Fast scanning also makes the flo~ 

imaging procedure much less sensitive to patient motion since differences of 

data acquired in very short intervals are taken.

WF66 

IMMOBILIZED FERRITE pAirri~ 1:'~: 5ELEL'rlVE SPOILING OF A HOMOGENF.OUS B o FIELD AND 

ITS APplICATION TO SLrI~A~ C01L $ ~ P Y . 

Y. Oeoffrion'. M. Rydw. I. C. P Smith sod H C. J~roU 

Division of BiololicaJ Sciences 

Nations/Research Council of Csosdt 

Ottawa, CANADA KIA 01~ 

Ferrite pa.,'ticles on • solid support have been used to achieve selective sod 

lo~ spoilinj of• homogeneous Bo field. IH ~ imNLini techniques sad 3ip 

surface coil studies on phantoms have been used to deLineste the proTde of the loca/ized 

perturbation of the Bo field sod to further demonstrste thst in the p~sont sppticstion 

the spoifin| effect is Limited to _~ 0,5 cm •ray from the surface of the immobi/o.ed ferrite 

particles. AppLication of this spproach to surface coU studies on a,nims/s has shoved that 

itvu feasible to discrimiatte between 31p resonsoces originttiaj from tissues near the 

body surface ofso soims/from those originttiag from tissues lyinj deeper in the 

mmlmml.

WF68 

The SWIFT Method for In Vlvo Localized Spectroscopy 

W.M. Chew, L.-H. Chang, T.L.dames* 

Department of Pharmaceutical Chemistry 

University of California San Francisco 

San Francisco, California g4143 

Of paramount Importance in in v/vo MRS studies is the ability to 

acqulre localized spectra from the region of interest and with maximum 

signal to noise. Failure to localize can lead to false results and erroneous 

conclusions. Spectra obtained using localization schemes that fail to 

maxlmlze signal to noise (S/N) can require long acquisition times and thus 

obscure the ability to detect physiological changes. The optimal strategy 

during the localization process is to keep manipulation of the magnetization 

from the region of Interest to a minimum, thereby minimizing the loss of 

S/N that can occur due to finite T2's and Instrumental imperfections. 

We present a method of localization using the SWIFT (Stored 

Waveform Inverse Fourier Transform) excitation method (1). Unlike most 

gradient localization methods (wlth one exception (2)), magnetization in the 

region of Interest is not manipulated (volume selective nonexcitation during 

the preparation period) thereby retaining full z magnetization, an important 

signal to noise consideration. Magnetization outside the region of interest is 

dephased and saturated using a combination of tailored SWIFT pulses and 

magnetic field gradients; a "read-out" pulse then interrogates spins left on 

the z axis from the region of interest. 

(i) A.6. Marshal, A.T. Hsu, W.W. HunLer Jr., P. Schmalbrock, Prec. Soc. Me~. Res. Med. FirLh Annual 

MeeLing, Montreal (1986). 

(2) D.M. DoddrelI, J.M. Bulsing, GJ. 6allowiy, W~. Brooks. J. Field, M. Irving, H. Baddeley, d. Magn. 

Res. 70(2), 31g (1986).

WF70 

NATURAl, ABUNDANCE CARBON-13 NMR IMAGING 

IN BIOLOCICAL SYSTEMS 

Donald W. Kormos 

Department of Radiology, University Hospitals, 

C~RU, Cleveland, Ohio ~I06 

and Hong N. Yeung 

Technlcare Corporation, 29000 Aurora Road, Solon, Ohio 44139 

The feasibility of natural abundance carbon-13 NMR imaging was 

evaluated. Spin-echo, undecoupled images were obtained at 4.7 T (Oxford 

Instruments, 33-cm bore magnet) using a broadbanded Technicare Teslacon 

MR imaging system. A cylindrical volume coll (= 3,500 cm 3) and a single- 

turn surface coll (3 cm diameter), tuned to 50.6 MHz, excited and 

received the carbon signals. Polypropylene spheres containing isotop- 

Ically enriched methanol (= 99%) and ethylene glycol with carbon-13 in 

natural abundance (= 1.1%) were used as phantoms for setting the imaging 

parameters. Natural abundance carbon-13 images were obtained from an 

unfertilized chicken egg and a fresh oxtail (both obtained at a local 

supermarket!). 

Phantom images clearly showed =image multiplicity" due to carbon- 

proton J-coupllngs. The chicken egg image depicted only the methylene 

(-CH2-) carbons of the egg yolk. This finding was confirmed by high- 

resolution carbon spectra of separated egg white and egg yolk. 

Similarly, transverse and saglttal carbon-13 images obtained from the 

oxtail phantom exclusively mapped lipid carbons. Separated fat and water 

proton images of the oxtail using a modified Dixon method (with in situ 

inhomogeneity correction) were also obtained. A very good correlation 

between the carbon-13 image and the proton fat image was observed. 

We conclude that natural abundance carbon-13 imaging is feasible at 

high fields with reasonable (= i hour) imaging times. Hardware 

improvements, proton decoupllng, and carbon-13 labeling will undoubtably 

decrease the degree of difficulty.

WF72 

THE DESCI~IPTII]N AND ELIMII~TION OF SUBTRACTION ARTEFACTS IN :H 

EDITING SCHEMES: A PHASE CYCLING SCHEME TO ELIMINATE ABSORPTIVE 

AND DISPERSIVE ERRORS 

H.P Hetherington °, D.L.Rothman, K.L. Behar, M.R. Bendall and R.G. Shulman 

Dept of Molecular Biophysics and Biochemistry 

Yale University New Haven C.T. 06510 

In the past three years there has been a rapid growth in the 

application of LH NMR to monitor in vivo metabolism. Due to the small 

chemical shift dispersion of the JH spectra, many small metabolite 

resonances are obscured by spectral overlap. To resolve these resonances 

a variety of homonuclear editing schemes have been proposed which rely on 

the use of a selective inversion pulse or CW decoupling to alter the 3- 

modulation of the edited resonance(1). However, these methods 

experimentally and theoretically fail to achieve exact cancellation of 

non-modulating resonances at the frequency position of the e~ited 

resonance, thereby resulting in quantitative errors. 

By use of matrix methods(2) and the product operator formalism (3), we 

have identified the source of these errors as arising fromthe editing 

pulse creating: a) perturbations in the absorptive refocusing 

magnetization due to off resonance spin inversion effects and b) 

dispersive refocusing magnetization due primarily to the effective field 

changes during the selective inversion pulse or ~ecoupling period. 

HoNever, these errors can be theoretically and experimentally eliminated 

by using the following sequence and appropriate cycling scheme, 

where e and 2e form a standard spin echo sequence, ee.~ is a selective 

inversion pulse, ~=I/23 for doublets, and ee.~*~e=~. The selective 

inversion pulse, e~s~, is applied on alternate scans to the 3-coupled 

spin of the resonance to be edited and to a position symmetrically 

disposed to the edited resonance to eliminate errors in absorptive 

refocusing magnetization. Incomplete cancellation due to dispersive 

refocusing magnetization is eliminated by cycling the sequence of pulses 

and delays (2e.~-~e-2e-~) according to the absorptive phase cycling 

described by Hetherington and Rothman(2). This scheme has been applied to 

the living cat brain at 4.?T to obtain an edited spectrum of lactate. 

I) D.Rothman et al, Proc. Natl. Acda. Sci, 81, 6330, (19B4) 

S. Williams et al, 3. Magn. Reson. bJ,40&, (19B5) 

2) H.Hetherington and D.Rothman, 3. Magn. Reson.,b5t 348,(1985) 

3) 0.Sorensen, Prog. Nucl. Magn. Reson. Spectrosc., 54,512,(1983)

WF74 

TAILORED EXCITATION IN THE ROTATING FRAME 

G.S. Karczmar*, T. Lawry, M.W. Weiner, 

J. Murphy-Boesch, and G.B. Matson 

Veterans Administration Medical Center, and 

University of California, San Francisco, California 

Shaped RF pulses are currently used in magnetic 

resonance imaging (MRI) to provide uniform excitation across 

a selected frequency interval. The distribution of 

frequencies across the sample is created by a gradient in 

the B 0 field. It is also possible to utilize a gradient in 

the RF (B 1) field for spatial discrimination. Here we 

describe a new approach to localized spectroscopy based on 

selective excitation of precessional frequencies about an 

inhomogeneous B 1 field. Selective excitation is produced by 

a second RF field, designated B2, which is orthogonal to the 

inhomogeneous B 1 field. This approach derives from Hoult's 

rotating frame selective pulses (1). However, it differs 

in that the B 1 and B 2 fields are not on continuously. 

Furthermore, the B 2 field is tailored to achieve uniform 

excitation over a desired frequency interval. 

In its simplest form, the experiment is initiated by 

application of a B 1 field along the X axis of the rotating 

frame, through an NMR probe which produces an inhomogeneous 

RF field. At multiples of time tau the B 1 field is 

momentarily removed and a brief B 2 pulse applied along the Y 

axis. The B 2 pulses are selective for precessional 

frequencies about B 1 which are multiples of 1/tau, and 

continuation of the sequence produces a net tipping of 

selected magnetization towards the negative Y axis. Halfway 

through the sequence the phase of the B 1 field is reversed, 

so that the experiment ends with selected magnetization 

along the negative Y axis, and all other magnetization 

aligned along the Z axis. The slice profile approaches a 

sine shape. Improvement of the selection profile is 

obtained through modulation of the duration of the 

individual B 2 pulses to obtain tailored excitation 

equivalent to that of shaped pulses such as the sine pulse. 

Computer simulations are used to demonstrate a variety 

of pulse sequences which achieve acceptable slice profiles 

while minimizing RF power. Advantages over other B 1 

localization experiments include improved uniformity of 

excitation over the selected slice, and minimal perturbation 

of magnetization outside of the selected slice. This makes 

multiple slice experiments possible. Extension of the 

method to the use of other shaped pulses is straightforward. 

1. D.I. Hoult, J. Magn. Reson. 38, 369 (1980)

WF76 

RAPID ~ F R A M E IMAGING 

Kenneth R. Metz* and John P. Boehmer 

Department of Radiology 

The Pennsylvania State University College of Medicine 

~he M. S. Hershey Medical Center 

P. O. Box 850 

Hershey, Pennsylvania 17033 

Since its introduction [Hcult, J~R, 33, 183 (1979)], rotating-frame 

imging (RFI) has excited growing interest. This technique employs 

radiofrequency field (B I) gradients to produce a spatial (x) dependence 

of the NMR nutation frequency: Fl(x) = ~Bl(X)/2~. Ordinarily, a one- 

dimensional spat/al image is formed using a t%D-dimensional pulse 

sequence of the genen~l type: 

(Preparation - n-P - FID Acquisition - Relaxation Delay) n [RFI] 

where the rf pulse width n-P increases with the number of stored FID's. 

2DPT processing with respect to the pulse width (t I) and acquisition time 

(t 2) yields a 2D frequency-dum~in map correlating the NMR spectrum along 

the F 2 axis with the spatial position along the F 1 axis. 

In many cases, the obserut~ chemical species (e.g., IH20 or 23Na+) 

may exhibit only a single spectral line. ~his allows the rotating-frame 

imge to be formed using the sequence: 

Preparation - (P - Acquire One Point) n - Relaxation Delay [Rapid RFI] 

where n s~ssi~ individual points are acquired between pulses (P) in a 

long train. The rapid RFI method uses only a small fraction of the rf 

power normally required, provides, good spatial resolution, and is 

extremely fast, as shown by the I~ image below for a three-c/hamber 

phantcm acquired in 41 ms. 

l ' ' ' i ' ' ' I ' ' 

6000 4000 2000 Hz

WF78 

A NOVEL METHOD FOR DIFFUSION AND FLOW MEASUREMENTS: 

IMAGING OF TRANSIENT MAGNETIZATION GRATINGS 

Timothy R. Saarinen* and Charles S. Johnson, Jr. 

Department of Chemistry 045A 

University of North Carolina 

Chapel Hill, NC 27514 

Holographic relaxation spectroscopy (HRS) is an optical 

method in which a grating pattern of photoproducts is written 

into a sample by a laser interference pattern. The time 

evolution of the grating is determined by diffusion, flow, 

and relaxation rates. Analogous PFG-NMR experiments are 

described in which sinusoidal patterns of magnetization are 

"written" into samples along the gradient direction. The 

time evolution of the "grating" with diffusion, flow, and 

relaxation present is determined. To monitor the time 

dependence, a "reading" gradient is applied during acqui- 

sition to yield an image of the "grating" after Fourier 

transformation with respect to the acquisition time. The 

Carr-Purcell sequence with an applied magnetic gradient is 

discussed along with applications to diffusion and flow.

WF80 

MULTIPLE QUANTUM FILTERING: USES IN IMAGING AND IMAGING RELATED 

EXPERIMENTS 

Nikolaus M. Szeverenyi 

SUNY, Health Science Center 

NMR Laboratory, Room 301 

708 Irving Avenue 

Syracuse, NY 13210 

Tel. (315) 473-8469 

The behavior of multiple quantum coherence in the presence of 

magnetic field gradients can be exploited as another mechanism to filter 

out water signal in an imaging instrument. Using a combination of 

r.f./receiver phase cycling and the selection of a particular echo, one 

can achieve a high level of water suppression. Lactic acid and to a 

lesser extent fat, are biological materials that respond to this 

experiment. Results using selective pulses are displayed with a 

discussion of sensitivity considerations, field dependence and possible 

applications.

WK2 

15N NMR OF MACROMOI_F.CULF-S: APPLICATIONS TO THE 

b"I'UDY OF PROTEINS IN SOLUTION 

M. Bogusky', P. Leighton, R. Schiksnis, A. Khoury, P. Lu and S. Opella. 



Philadelphia, Pennsylvania 19104 

One- and two-dimensional heteronuclear NMR techniques 

combined with 15N biosynthetic labelling have been used to study a variety 

of globular and membrane bound proteins in solution. Five proteins 

including the fd and Pfl phage coat proteins in micelles, cro repressor, lac 

repressor and lac headpiece, covering the molecular weight range 

6-155kD have been investigated using these techniques. Heteronuclear 

correlation, both nitrogen and proton observe are used to resolve amide 

nitrogens and protons as well as sidechains containing nitrogen. 

Assignment of resonances to amino acid type are completed through the 

use of single site 15N biosynthetic labelling. Sequence specific assignments 

are accomplished with the use of 13C-15N double labelled samples. 

Evaluation of the advantages and limitations of both heteronuclear 

correlation techniques with regard to molecular weight are presented. 

Applications of polarization transfer techniques are used to 

increase sensitivity, assign resonances and monitor proton exchange for the 

labelled proteins discussed. Protein backbone and sidechain dynamics are 

characterized by the heteronuclear 15N-(IH} NOE. Qualitative 

determination of protein mobility on the nanosecond timescale is readily 

accomplished for moderately sized proteins using the heteronuclear NOE. 

Proteins dynamics are also characterized with the use of "dynamic filters" 

inherent in several heteronuclear multipulse experiments. The combination 

of the heteronuclear techniques discussed with the conventional proton 

NMR techniques extend the molecular weight range of protein systems 

which become tractable by high resolution solution NMR.

WK4 

P.E.COSY, DOUBLE QUANTUM FILTERED RELAY SPECTROSCOPY AND MORE. 

Stephen C. Brown, Paul L. Weber & Luciano Mueller 

Smith Kline & French Laboratories 

709 Swedeland Road, Mail Code L940 

Swedeland, Pennsylvania 19479. 

Whenever one gains the impression that some aspect of NMR is 

becoming exhausted, a new twist is stumbled upon that opens up new 

avenues of research. For instance, we recently found a new procedure 

to purge the phases in COSY spectra, which we subsequently utilized to 

generate E.COSY 1 type spectra. This experiment involves the reduction 

of the flip angle in the mixing pulse combined with the said phase 

purging. The resulting spectra looked impressive enough to leave the 

impression that some people may want to see a name associated with 

this procedure; how about primitive or P. E.COSY 2. 

We also applied dual double quantum filtering procedure to the 

RELAY experiment as originally proposed by O. Sorensen 3. To our 

delight we obtained superb results in a small protein (ubiquitin), 

which suggests that this procedure may become the standard RELAY 

technique. For people who are in desperate need of names may we call 

this DQFRELAY or DRECKSY (true meaning to be revealed upon request). 

Furthermore, we found an optimized combination of selective 

excitation and homogeneity spoiling in the 2DNOE experiment to 

suppress the solvent peak in H20 solution. These results and more we 

wish to present. 

References: 1. C. Criesinger, O. W. Sorensen and R. R. 

Ernst, J. Amer. Chem. Soc. 107, 6394 (1985). 

2. L. Mueller, J. Magn. Reson., March 1987. 

3. O. W. Sorensen, Ph.D. thesis, ETH #7658 

(1984).

WK6 

ISOTOPE-FILTERED PROTON NHR EXPERIMENTS 

FOR SIMPLIFYING COMPLEX SPECTRA 

Stephen W. Fesik* Robert T. Gampe, Jr. Jay R. Luly, Herman H. Stein and 

• ' t 

Todd Rockway. Pharmaceutical Division, Abbott Laboratories, Abbott Park, IL 

60064. 

Extracting structural information from proton NHR spectra of large 

btomolecules or molecular complexes can be extremely difficult due to the 

severe overlap of many signals. Recently, however• experimental approaches 

have been introduced to overcome some of these limitations by selectively 

detecting protons attached to an isotopically labelled nucleus (1,2) as well 

as their scalar (2) or dipolar coupled (3) partners. Isotope-filtered 

homonuclear Hartmann-Hahn (HLEV-17) and NOE experiments in which a spin-echo 

difference pulse sequence was inserted in the experiment are presented. The 

approach is illustrated using an 15N-labelled dipeptide and applied in a study 

of the bound conformation of an isotopically labelled pepsin inhibitor. In 

addition, isotope-filtered 2D NOE spectra are presented of a large, 15N- 

labelled cyclic peptide analog of atrial natriuretic factor incorporated into 

a model membrane. From the spectral simplification achieved in the 

experiment, additional proton-proton distances were obtained unambiguously, 

aiding our structural studies. 

I. R.H. Griffey, A.G., Redfield, R.E. Loomis, and F.W. Dahlquist, 

Biochemistry, 24, 817-822 (1985). 

2. J.A. Wilde, P.H.Bolton, N.J. Stolowich, and J.A. Gerlt, J. Magn. Reson., 

6__88, 168-171 (1986). 

3. R.H. Griffey, M.A. Jarema, S. Kung, P.R. Rosevear, and A.G. Redfield, 

J. Am. Chem. Soc., i0___~7, 711-712 (1985).

WK8 

ISOTROPIC MIXING IN DNA 

Peter F. FIynn', Agustin Kintanar, Gary P. Drobny 

and Brian R. Reid 

Department o] Chemistry, Uniuersity of Washington 

Seattle, WA 98195 

We have investigated homonuclear coherence transfer in synthetic DNA oligonu- 

cleotides using two-dimensional isotropic mixing experiments. These experiments 

employ broadband homonuclear decoupling techniques (MLEV-16) during the mix- 

ing period to induce isotropic coupling within a spin system resulting in net trans- 

fer of coherence. The length of the mixing time determines the extent of coherence 

transfer; brief mixing periods lead to COSY-like spectra and at longer mixing times, 

relayed coherence transfer effects are introduced. 

This method was used to determine the scalar connectivities of sugar protons 

in canonical B-form, bent, and hairpin DNA structures. Cross-peaks were assigned 

unequivocally without recourse to structural assumptions, since coherence is trans- 

ferred only through bonds. Assignments derived from these experiments were used 

to simpli~" and confirm NOESY spectrum assignments. 

Isotropic mixing techniques as applied to oligonucleotides differs from conven- 

tional relayed coherence transfer techniques in that one can simultaneously observe 

shor~ and long range coherence transfer within a spin system using the former 

method. In addition, long range coherence transfer is more easily observed using 

isotropic mixing.

WKIO 

IH, IsC, AND ISN NMR STUDIES OF METAL COMPLEXES OF BLEOMYCIN 

Ian J. Mclennan* Michael P Gamcslk, Susanta K. Sarkar, Ad Bax t , and 

I ° 

Jerry D. Gllckson, Depar ~ment of Radiology, The Johns Hopkins University 

School of Medicine, Baltimore MD 21205 and SNatlonal Institutes of Health, 

Bethesda MD 20892. 

The solution conformation of the Zn(II) bleomycin complex has been 

studied by ZH, IsC, and ISN NMR. As part of the study we have performed 

rotating frame NOE experiments in both H20 and D20. The Zn(II) bleomycln 

complex has been found to be partlcularly amenable to rotating frame 

experiments since the TlP'S of the complex are long (-50ms) at 4°C. The 

complete assignment of the IH spectrum of the Zn(II) bleomycln complex has 

been accomplished by COSY-llke experiments utilizing Hartman-Hahn 

polarization transfer. The complete assignment of the IsC spectrum of the 

Zn(II) bleomycin complex has been accomplished using the RELAY method 

(Lerner and Bax (1986) J. Magn. Reson. 69, 375). The assignment of the 

peptide amlde nitrogens in free bleomycin and the Zn(II) bleomycin complex 

was accomplished by IH-16N multiple quantum experiments. The results from 

these experiments are discussed in terms of a probable solution 

conformation of the Zn(II) bleomycln complex.


QUANTITATIVE INTERPRETATION OF A SINGLE 2D NOE SPECTRUM 




A new method is suggested for the quantitative in- 

terpretation of 2D NOE data using selective relaxation rates 

and matrix techniques. This approach reduces the experimen- 

tal time from one week to one day, gives proton-proton dis- 

tances with a precision of I0.1 ~, and can be used to 

characterize the internal dynamics. With this approach the 

structural and dynamic properties of Gramicidin S were 

determined from a single 2D NOE spectrum with a mixing time 

of 0.2 s. The peak volumes in the 2D experiment were scaled 

via the measured selective relaxation of Phe NH and Orn H ~ 

protons and the matrix of scaled peak volumes was solved to 

yield the relaxation rate matrix. The distances measured by 

this approach were indistinguishable (I0.1A ) from those 

measured from 1D NOE experiments, the buildup of cross peaks 

in the 2D NOE experiments, and the distances expected from 

the crystal structure. The dynamics were determined from 

the ratio of the sum of all the cross relaxation rates to 

the rate of decay of the diagonal peak which, for isotropic 

motion, depends only the the correlation time. This 

analysis showed a correlation time for the NH and H ° protons 

of 0.9~0.1 nsec; the close correspondence between the ob- 

served and expected values show that the peptide backbone is 

rigid in solution over the time scale of molecular tumbling. 

Internal motions of make a significant contribution to the 

relaxation of some side chain groups. The implications and 

limitations of this approach and the applications to DNA 

structure determination will be discussed.

WKI4 - POSTERS 

SYMMETRY AND ANTISYMMETRY IN 2D NMR SPECTRA 

O.W. S6rensen, C. Griesinger, C. Gemperle 


Laboratorium fSr Physikalische Chemie 

EidgenSssische Technische Hochschule 

8092 Z~richo Switzerland 

The conditions for obtaining 2D spectra symmetric or 

antisymmetric with respect to reflection about the 

diagonal have been extended and generalized. They 

can be formulated either in terms of the structure 

of pulse sequences or in terms of the coherence 

transfer pathways selected. 

Recent results indicate that new experimental 

techniques producing antisymmetric or asymmetric 2D 

spectra can be of advantage in certain practical 

situations. For example, experiments leading to 

antisymmetric spectra often result in suppression of 

uninformative and disturbing diagonal peaks.

WK16 

MULTINUCLEAR SOLID STATE NMR STUDIES OF INTERNAL MOLECULAR DYNAMICS IN 

FIBROUS AND CRYSTALLINE PROTEINS 

Y. Hiyama*, J. W. Hack +, S. W. Sparks** and D. A. Torchla, 

Natlonal Institute of Dental Research, Natlonal Institutes of Health 

Bethesda, Maryland 20892 

Collagen*: Intact rabbit Achilles tendon collagen containing 

4-fluorophenylalanine (provided by Dr. J. T. Gerlg) has been studied by 

19F NMR at 470 MHz. Analysls of the 19F CSA powder patterns obtained at 

-37°C show that motion of all amino acid sldechains is restricted to small 

angle rolling or rare 180 ° fllps of the phenyl ring. In contrast, above 

-4°C, the powder pattern indicates considerable heterogenlety in the 

dynamics of the sidechaln, a result that will be discussed with reference 

to collagen fiber structure. 

Keratin+: Assembled intermediate filaments of mouse epidermal 

keratin, labeled with 13C and 2H (provided by Dr. Peter Steinert) have 

been studied at several field strengths. Analysls of measurements of 

Tl'S, llne widths and NOE values of filaments labeled with [I-13C] and 

[2-13C] glyclne show that the protein backbone, in the non-helical N- and 

C-terminal domains, is Isotropically mobile on the nanosecond timescale. 

Deuterium llneshapes of leucyl residues, located in the interior helical 

domain of the protein show that motions of these sidechains are 

anisotropic. We will report on the spatial extent and timescale of these 

sidechalr motions based on our analysis of the 2H lineshape and relaxa- 

tlon data. 

Staphylococcal Nuclease~'#: Using genetically engineered E. Coli 

(provided by Dr. J. Gerlt) we have prepared crystals of S. Nuclease 

containing residue specific NNR spin labels. Deuterium lineshapes show 

that except for methyl rotation, molecular motion is highly restricted at 

temperatures below -35°C. In contrast, at 20°C, at least one half of each 

of the Pro, Met, Phe and Tyr residues execute large amplitude sidechain 

motions. The detailed nature and timescale of these motions will be dis- 

cussed and, where possible, related to the crystal structure. These are 

the first extensive measurements of internal motions in a protein crystal 

and clearly show that even in crystals proteins are dynamic structures.

WK18 

21) NMR METHODS FOR ~ SYSTEM IDENTIFICATIDN IN LARCE 

PROTEINS 

CLzudi~ Dalvi% S.S. Naru~* and Peter E. Wright 

Department of uc~ecular 

R ~ I m ~ of Scripps 

1~ North Tcrr~y Pines Road 

Recent deve~pments in 2D NMR method~y now make it possible to 

obtain extensive and ~m~=uous spin system assignments for ~ of 

malecmlar weight up to- 20,O00d. Phase sensi~ve double quantum spe~:~Fy 

and Hartman-Hahn techniques are particularly im~l~ Appli~ticvs of these 

OdS to ]~g~emog]~l~n (M- 16,000) and myog~l~n (M ~ 18,000) wi~ be 

• Acc~n of dc~l~ quantum spectr~ wi'~ d~f&~nt • values 

impcm-tant to a.1]Dw di~erenl~ d direct and r~mote connectivj.i~.es and for 

spectr~ mmpl~f-ic~,',n and edii~ng. The double quan~nn experiment is 

well,bred for detection of weak, ]c~g-~d~ge ~ and can ~ e 

una.mhiguous czmuectiv'ities between the aroma~c and alipha~c ~ of 

~ e spin systems. R ~ frame NOESY experiments are inva.luahle in 

studying exchange troces~s between different conforma~kmal suhstates of 

]~emq~hin. We show that Hart~an-Hahn coherence transfer experiments 

can be used to ~d~ amino acid spin systems in a ~ of malecular 

weight 38,000; a::mv~ COSY techniques are iI~r~.~le far a ~ of 

size.

WK20 

ImQm~ss ~ M~/TIDIM~SIGNAL ~ C NMR 

H. Armitage, U. Bl6mer, I. Genge, A. Khuen, and D. Ziessow 

I.N. Stranski Institute, Technische Universit~t Berlin 

i000 Berlin 12, West Germany 

Stimulus to the osntinuing development of M~DI~4 (MUltidimensional Stochas- 

tic Method) is the simplicity of the measurement process and the prospect 

to obtain 2D spectra with high digital resolution which, with conventional 

2D techniques, ~uld require the processing of i0 or more Giga~rds data 

arrays. 

In order to take full advantage of the method, hardware and software has 

been developped which allows the continuous recording of data pairs for the 

excitation ( special ly designed quaternary noise) and response time func- 

tion, 1 Me~apair or more depending on the amount of DRAM plugged into the 

VME bus of the 68000-based computer system for data acquisition. Spectral 

information is obtained by correlation of excitation and response as 

formed in the frequency dom~J_n with the ais of a Honeywell BulISPS 9 ~ 

cc~puter. First order oprrelation yields the c~mDn ID spectrum Hl(W). Ex- 

tremely long time records are used in order to alleviate artifacts stemming 

from cyclic correlation. From the same raw data, after suitable subtraction 

of the first order response, third ~ ~ is performed pointwise 

to determine a genuine 3D spectral function H3(Wl,W2,W 3) in regions of in- 

re_rest as indicated by the ID spectrum. For instance, the choice w3=-w 2 re- 

duces H 3 to a 2D spectrum H 3 ' (Wl,W 2) which is equivalent to the result of 

the E-COSY technique. Points my be selected such that the entire spectral 

range is assessed with coarse digital resolution, and narrow regions with 

extremely small frequency steps. 

Simulated and experimental data are presented to demonstrate the unique 

features of MUDI~4. As a particular case study, results for the cyclic pep- 

tide cyclosporin are shown which derive frcm 80 Megapairs raw data for a 

total spectral range of 3246 Hz (7.5 h magnet time). A typical 2D spectrum 

(512x512 window at 0.4 Hz step size) is given which ~uld require the pro- 

cessing of about 256 Megawords of data with conventional 2D techn/ques.


SOLVENT SUPPRESSION WITHOUT PHASE DISTORTION 

Malcolm H. levitt* and Hazy F. Roberts 

M.I.T., NN14-5122, Cambridge, MA 02139 

Ve describe a new class of pulse sequences, NERO (Non-linear Excitation 

Rejecting On-Resonance), which alloy wideband excitation of an NI~ 

spectrum except for a deep, flat section near the carrier vhere the 

response is zero. The novel feature of the nev sequences is that phase 

distortion of excited resonances is negligible, in contrast to usual 

methods based on linear response. Ve rill shov numerical simulations 

and experimental results for the following sequence, called NER0-1: 

120°-~1-115°-~2-115 °-2~3-115°-~2-115 °-¢1-120°-~ r 

where pulses 180 ° out of phase have an overbar, and delays ~k are given 

by 

~1 = 0. 1391(~0exc12n) 

.c 2 = 0.6251( It~xc1210 

2~ 3 = 0.4281(&0exc/2n) 

~r = 0" 2221(A~exc/2~) 

Here (A~0exc/2,) is the offset frequency (Hz) of the center of the 

excited spectral region. This class of pulse sequence is capable of 

providing solvent suppression almost free from undesirable phase 

distortions.

WK24 

BROADBAND HETERONUCLEAR DECOUPLING 

IN THE PRESENCE OF HOMONUCLEAR INTERACTIONS 

D. Surer*, K.V. Schenker and A. Pines 


Heteronuclear decoupllng in anlsotropic systems llke solids and liquid 

crystals has to compete not only with the offset from resonance of the 

radio frequency and the heteronuclear couplings, but also with strong 

homonuclear interactions like homonuclear dipole-dipole couplings or 

quadrupolar interactions. These additional interactions make the 

decoupling performance of CW decoupling strongly offset dependent and 

are not overcome by the composite pulse decoupling sequences developped 

for isotropic liquids. We have developped a theoretical analysis of 

decoupling in such systems and found a class of composite pulse 

decoupling sequences designed for use in anisotropic systems that are 

relatively insensitive to resonance offset and pulse imperfections. One 

of the sequences, COMARO-2, can be written as YX YX YX YX YX ~, where 

each element represents a composite pulse 385 320 25. 

sl 

/ _\ 

lg 

• -" .-•'" 

Figure : Left : theoretical offset dependence of deuterium decoupling 

for a single deuteron. Right : experimental results from 

dimethoxybenzene-d 8 in a nematic liquid crystal. 

References : 

D. Suter, K.V. Schenker and A. Pines, J. Magn. Reson. (Hay 1987). 

K.V. Schenker, D. Surer and A. Pines, J. Magn. Reson. (Hay 1987). 

CW 

2

WK26 

LINE SHAPES IN ONE-DIMENSIONAL 

CHEMICAL SHIFT IMAGING 

P.B. Barker W, D. Bailes a, D. Bryant a and B.D. Ross 

Huntington Medical Research Institute, Pasadena, CA 91105. 

aplcker International, Wembley, Middlesex. 

It has recently been demonstrated that the two-dimensional NMR 

technique of Marecl (I) gives good spatially locallsed 31p spectra In 

clinical applications (2). In some instances the spectral resolution may be 

degraded by the "phase-twlst" line shape (3) which is encountered as a 

result of the phase-modulation of the NMR signals as a function of their 

spatial coordinates 

This poster presents a variation of the data processing methods 

developed in conventional high-resolution NMR to retain pure absorption 

llneshapes (4). The method requires the recording of two data sets for 

each phase-encode gradient amplitude; in one case the gradient amplitude 

is positive, in the other negative. These two data sets are then processed 

conventionally using complex Fourier transformations; linear combinations 

• of the two frequency domain data matrices are then used to cancel the 

dispersion components of the line shape. Other equivalent processing 

methods are possible; for instance, linear combinations of the original 

time-domain data matrices may be used in conj.unction with the 

processing method of States (5). Whilst this is slightly more efficient in 

terms of processing time and disk storage, the method used largely 

• depends on the ease-of Implementation on the available spectrometer 

system.The improvements offered are expected to be particularly 

noticeable In the extension to multl-dlmenslonaI chemlcal shift Imaging. 

( 1 ) T.H. Mareci and H.R. Brooker, J. Magn. Reson., 57, 157 (I 984). 

(2) D. Bailes et. al., J. Magn. Reson., submitted for publication 

(3) G. Bodenhausen, R. Freeman, R. Niedermeyer and D.L. Turner, J. Magn. 

Reson., 26, 133 (1977). 

(4) J. Keeler and D. Neuhaus, J. Magn. Resort., 63, 454 ( ] 985). 

(5) D.J. States, R.A. Haberkorn and D.J. Ruben, J. Hagn. Resort., 48, 286 

(1982).

WK28 

SELECTION OF COHERENCE TRANSFER PATHWAYS BY FOURIER ANALYSIS 

HOW TO IMPROVE THE EFFICIENCY OF 2D NMR SPECTROSCOPY 

R. Ramachandran, P. Darba and L.R. Brown* 

Research School of Chemistry 

The Australian National University 

Canberra, A.C.T. 2601, Australia 

To interpret complex 2D NffR spectra it is often necessary to run 

a series of complementary 2D N~ spectra which select for different 

kinds of information. Examples would be a series of auto correlated 

spectra with filters of different quantum orders or a series of 

multiple quantum correlation spectra of different quantum orders. As 

currently practiced, each member of the series is recorded separately 

using concurrent cycling of pulse and receiver phases to select the 

appropriate coherence transfer pathway. This is a very inefficient 

procedure which requires large amounts of spectrometer time and which 

leads to spectra that may not be strictly comparable due to 

instability of the spectrometer and/or the sample. 

A method will be shown for extracting such a series of spectra 

from a single data set. The new method involves recording a series 

of spectra with appropriate incrementation of pulse phases, but with 

no variation of receiver phase. Fourier analysis of the set of 

spectra by means of digital zero-order phase corrections then allows 

extraction of coherence transfer pathways containing any specific 

multiple quantum order from the same data set. Examples will be 

given for generation from a single data set of multiple quantum 

filtered COSY spectra of different quantum orders and multiple 

quantum spectra of different quantum orders. 

A major advantage of the proposed method is that every transient 

recorded is used in the generation of the spectum corresponding to 

each quantum order. This means, for example, that compared to 

recording a COSY spectrum with a two-quantum filter by conventional 

means, there is no penalty in sensitivity involved in generation of 

multiple quantum filtered spectra with filters of order 2,3 and 4 (or 

more) by the proposed method. This also makes the new method highly 

efficient for experiments which require co-addition of spectra 

corresponding to different quantum orders, e.g.E. COSY or time 

reversal. An example will be shown for E. COSY.

WK30 

PATTERN RECOGNITION IN 2D NMR. 

A MULTIVARIATE STATISTICAL APPROACH WITH LOGIC PROGRAMMING. 

H. Grahn , F. Delaglio, M. A. Delsuc and G. C. Levy, 

NMR and Data Processing Laboratory, Bowne Hall, 

Syracuse University, Syracuse, NY 13244-1200 

A new method for the analysis of two-dimensional NMR data 

is presented. The method, based on principal component 

analysis (PCA), is shown to be very efficient in the 

modeling of different spin patterns in homonuclear shift 

correlation 2D spectra. 

The PCA method can be described as a graphical method 

which projects multidimensional data down on a few 

dimensional space (line, plane or hyperplane) and hence 

provides a simplified interpretation of the clusters in an 

n-dimensional space. The scope of the method is that similar 

objects (spins) can be grouped together. Based on a prior 

knowledge of different spin systems, new "unknown" compounds 

can be classified and the spin connectivities in the molecule 

can be outlined. 

An important difference to other pattern recognition 

methods is that no previous assumptions about the analyzed 

data are needed, e.g., coupling constant information. The 

method uses the intensities of the cross-peaks and the 

chemical shifts of the diagonal peaks as parameters. The 

first step in analysis is the preprocessing of the data. This 

step involves locating all peaks in the data and scaling peak 

intensities to unit variance. The peak data are reduced to a 

system of objects and variables for the PC analysis. In the 

course of the PC analysis, n-dimensional projections of the 

data are constructed which contain patterns which will group 

all the objects comprising each spin system into a 

characteristic pattern. Using the logic programming language 

PROLOG, the patterns can be located and the corresponding 

spin systems identified. 

Using PC analysis in combination with logic programming, 

it is possible to identify the different spin systems in a 

spectrum having mixed spin systems. 

We acknowledge NIH Grant RR-01317, N.A.T.O. for support of 

Dr. Delsuc and Troedsson Research Fund, Sweden, for support 

of Dr. H. Grahn.

WK32 

C~4IC~L EXCHANGE IN METAL £X/JSTE~. 

ANALYSIS WITH 2D LINEAR PREDICTION 

AND DIRECT ANALYSIS OF THE RATE MATRIX. 

Bruc~ A. ~ ' , J. A. Mallkayil, m~d Ian M. Azmltag~ 

Depa~ :,,-~-,L,~ of Mblecular Biophysics and Biochemistry 

snd Diagnostic Radiology 

Yale Urul.ver~l.ty School of M~dicine 

Nma Haven, CT 06515 

NMR methcKis are well suited tD the mMsurEm~nt of c~mnical exchange 

~ . In many ~ , ~ , such as the less sensitive metal 

nuclei that may be found in blomolecules, low signal to noise ratio may 

significantly hamper the aommrate msasure of exchange rates. To 

ov~-~ome this ~ have applied ~o recen%ly repcn-hed methods o£ NMR data 

analysis in these areas. As an alternative to the Fourier transform, 

we used the method of linear prediction with the s/ngular value 

deocmposit/nn (LPSVD) I . This method is potentially capable of 

signal fru, noise in the time series data, resulting in 

a noise free result. ~ , ~ have used the method for two- 

dimensional arm~lysis where its ability to elim/nate truncati~ 

artifacts allows the use of fe~.r points in t2 and in %/. This reduces 

the size of the 2D data set and minimizes experimsntal time. Analysis 

in this way gives directly the amplitude of the peaks required for the 

chemical exchange calculations without the need for integration. As 

apodization funct/ons are not used, there is no resulting distortion of 

peak intensity which might occur with normal 2D FT processed data sets. 

For both the one and %~o dimensional analyses with LPSVD, we polish the 

output data (frequency, dscsy, phase, and amplitude) with a non-lirear 

minimization. The calculated peaks from a single 2D data set are then 

used %o form a matrix of intensities that is analyzed using a recently 

described matrix dia~mLlization p r ~ . 

We will illustrate the use of this method with the analysis of metal 

excha~/8 in the dscanuclear cadmium-i±iolate complex, 

C~0(SO~O~O)*s(N~ )4" In the solid state, three distinct Cd sites 

have been identified in the sulfate form of this complex by X-ray 

crystallography and by solid state 1'3Od NMR s~-troscc~py- The three 

sites, site A, site B, and site C have Oi~, OdS4, and CdS40 

oocrdinations respectively 3 . In solution, site B and site C are in 

fast exchange and therefore a single 113 Cd resonazK~ is observed for 

these sites" The results of our 2D chemical exchange studies have 

further established, for the first time, metal exchange between site A 

and the other two sites. It is the kinetics of the latter exchange 

that we will describe using the oombined LPSVD and the matrix 

diagm~alization proosdures described above. 

i) ~Jsen, H. 1985, O. Mag. Res. 61:465 

2) Perrin C. L. and Gipe, R. K. J. Am. Chem. Soc. 106:4036 

Johnston, E. R. and Chert, D. 2~ h ~C ~ Abstract. 

Abel, E. W. et al. 1986, J. Mag. Res. 70:34 

3) Murphy, D.P. et al. 1981, J. Am. Chem. Soc. 103:4400 (and 

ref therein)

WK34 

DECONVOLUTION OF HIGH RESOLUTION TWO-DIMENSIONAL 

NMR SIGNALS BY DIGITAL SIGNAL PROCESSING WITH" 

LINEAR PREDICTIVE SINGULAR VALUE DECOMPOSITION 

David Cowburn. Adam E. Schuasheim, and Francis Picart 

The Rockefeller University, 

New York, New York, 10021 

NMR signals from high resolution pulsed experiments can be adequately represented by sums of 

sinusoids. Normally these signals are transformed to the frequency domain by FOurier transformation 

and the chemical information inherent in the frequency, damping, intensity, or phase of the sinusoids is 

subsequently obtained by various deconvolutions, ranging from simple 'peak-picking' for frequency to 

non-linear least squares fitting to obtain all the sinusoid properties. This deconvolution in the frequency 

domain is particularly compficated by the need to set initial parameters for the non-linear least squares 

analys~. The characteristics of the coatribufing sinusoids in the lime domain are needed for recognition 

of patterns of signals and correlation with expected properties. We show a new method of analyzing 

two-dimensional NMR spectra for this purpose. 

The technique of linear predictive singular value decomposition 0..PSVD), applied previously in 

NMR (1), permits the extraction of frequency information from a time-domain signal. The technique is 

related to the Fourier Transform and presents the same information but in a sometimes more useful 

fashion for certain types of processing with some costs in initial processing speeds. 

In our approach, a Fourier transform is performed as a digital filter on each row in the tl,t 2 space. 

The resulting interferogram is then passed column-by-cohtmn through the LPSVD algorithm. The 

information returned from the procedure is stored in a linked-list data file su'ucutre containing the 

amplitude, frequency, damping, and phase of the roots extracted for each column as well as a declara- 

tion field. A flexible structure is developed which employs a number of routines to process the roots 

and remove spurious results. 

We have found that these procedures can provide previously unobtainable resolution enhance- 

men), and eliminate sinc modulation caused by signal truncation. The procedure can obviate the need 

for t l-phase sensitive detection, and can substantially increase the apparent SNR of final spectra. Addi- 

tionally, the automated exwaction of chemical information can be facilitated by virtue of the resulting 

linked list of roots. These points are illustrated here with both simulated data and simple sets of experi- 

mental data. 

Acknowledgments 

Supported by grants from NSF, NIH, the Keck Foundation, and an equipment grant from Sperr3' 

Corporation. We are grateful to Dr. Dennis Hare, and to Dr. R. De Beer for provision of source codes 

for their programs, and Computing Services, Rockefeller University, for advice. 

481 

(1). H. Barkuijsen, R. de Beer, W. M. M. J. Bovee, and D. van Ormondt J. Magn. Res. 61 465-

WK3C 

LINEAR PREDICTION Z-TRANSFORM (LPZ) SPECTRAL ANALYSIS 

WITH ENHANCED RESOLUTION AND SENSITIVITY 

J. Tang* and J. R. Norris 

Chemistry Division, Argonne National Laboratory 

Argonne, IL 60439 

We have developed a new approach of spectral analysis (LPZ) l"s with improved 

resolution and sensitivity by combining the linear prediction (l~P) theory and the 

z-transform, a combination of Fourier and Laplace transform. Instead of using the 

power spectrum formula obtained by the conventional MEM method, the LPZ 

formula should be used to obtain a spectrum with phase information. The linear 

prediction coefficients can be calculated by the Householder decomposition 

(QRD) 1-~, the singular value decomposition (SVD), the autoregression method (AR) 

using the Levinson-Durbin algorithm or the Burg's algorithm s. The LPZ method 

can overcome the truncation artifacts and phase distortion problems. Applications 

of the LPZ method to I-D and 2-D NMR signals will be demonstrated. In addition, 

the comparisons among many variations of the LPZ method (using SVD, QRD or 

AR) and the other similar methods such as LPQRD 4, LPSVD s and the ME..M 6"7 

methods will be illustrated. 

1. J. Tang and J.R. Norris, J. Chem. Phys. 84, 5210 (1986). 

2. J. Tang and J.R. Norris, J. Magn. Reson. 69, 180 (1986). 

3. J. Tang and J.R. Norris, Chem. Phys. Lett. 131, 252 (1986). 

4. J. Tang, C.P. Lin, M.K. Bowman, and J.R. Norris, J. Magn. Reson. 62, 167 

(1985). 

5. H. Barkhuijsen, J. de Beer, W.M.M.J. Bovee and D. van Ormondt, J. Magn. 

Reson. 61, 167 (1985). 

6. J.P. Burg, Thesis, Stanford University (1975). 

7. S. Sibisi, J. Skilling, R.G. Brereton, E.D. Laue and J. Staunton, Nature 311, a46 

(1984). 

This work was supported by the Division of Chemical Sciences, Office of B~_~ic 

Energy Sciences of the U.S. Department of Energy under contract W-31-109-Eng-38.

WK3S 

EXPERIMENTAL STUDY OF THE OPTIRIZED SELECTIVE RF PULSES 

Jintong Haoo, T.H. hreci, K.E. Scott and E.R. Andrev 

Departments of Radiology and Physics 

Gsinesvllle, FL 32611 

Selective rodiofrequency (rf) pulmes ore important in both NHR 

spectroscopy end imaging. Because the magnetization equation of 

motion is nonlineor, the design of the rf pulse shapes cspoble of 

precisely affecting the magnetization in a veil-defined frequency 

range is not s simple problem. Recently, the concept of optimal 

control hob been introduced for the design of rf pulses amplitude 

modulated as a function of time to provide frequency selectivity. 

Several selective pulse shapes hsve been developed using these 

tethods, hoverer, very few experimental results have been presented. 

We have presented a detoiled description of the use of the conjugate 

gradient method in the optics1 control problem to design a selective 

180 degree inversion pulses (1). Using this method, we have found a 

series of the 9e and the 180 degree rf pulse shapes that have very 

high selectivity. We have performed experiments on I GE CS1-2 

imager/spectrometer vhich confirm theoretical predictions from the 

application of optimal control methods. Both our computer 

simulations end experimental results are presented in this poster. 

Also, we 8how that the frequency response of the magnetization 

affected by a selective 180 degree inversion rf pulse is the game as 

that for a selective refocusing pulse. Computer simulations for both 

a sinc and optimal pulse are presented to demonstrate the principle 

and experimental results for selective refocusing pulses ire 

presented. Thus, I single optimal selective 180 degree rf pulse can 

be used is either in inversion or refocusing pulse. In both 

IituationI, its selectivity can be optiIlzed to fit the desired 

frequency profile end we rill diicuII how to apply thlI procedure in 

designing selective pulses to fit various selectivity criteria. 

Optimal control methods can also be applied to the case of 

selective 90 degree rf pulses. The degree of improvement possible is 

not as great as for selective 180 degree pulses but significant 

improvement is possible. Both experimental and computer simulation 

results of the optimal selective 90 degree rf pulses will also 

be presented in this poster. Thus, the optimal control sethod has 

solved the problem of designing optimized rf pulse shapes for 

frequency selective excitation. 

This research is supported by grants from the National Znstitute of 

Health {P41-RR-e2278) and the Veterans Administration Medical 

Research Service. 

1. Jintong Meo, T. H. Mareci, K. N. Scott and E. R. Andrev, J. MIgn. 

ReIon. 70, 31e (1986)

WK40 

PULSE SHAPING FOR SOLVENT SUPPRESSION AND 

SELECTIVE EXCITATION IN TWO-DIMENSIONAL AND 

MULTIPLE PULSE NMR SPECTROSCOPY 

Mark McCoy, Laura Kang and Warren S. Warren* 


Applications of shaped radiofrequency pulses to solvent 

suppression in COSY spectra, excitation of two separate resonance 

frequencies, and uniform spin-1 excitation will be presented. We will 

also experimentally demonstrate the tradeoffs between symmetric 

amplitude modulation, asymmetric amplitude modulation, and 

simultaneous phase/amplitude modulation. Recent results of new 

analytical solutions to the Bloch equations, derived for atomic laser 

spectroscopy, will also be experimentally tested. 

This work is supported by the National Science Foundation 

under grant CHE-8502199. 

1. M. McCoy and W. S. Warren, Chem. Phys. Lett. (in press) 

2. F. Loaiza, M. Levitt, M. McCoy, M. Silver and W. S. Warren, J. Chem. 

Phys. (submitted)

WK42 

RELAXATION-ALLOWED COHERENCE TRANSFER 

BETWEEN SPINS WHICH POSSESS NO MUTUAL SCALAR COUPLING 

Stephen Wimperis and Geoffrey Bodenhausen 

Institut de Chimie Organique 

Universite de Lausanne 

Rue de la Barre 2 

CH-1005 Lausanne 

switzerland 

In NMR of isotropic liquids it is often stated 

that coherence transfer can only occur between two spins 

that possess a mutual scalar coupling. This assertion is 

put to frequent use, for instance in two-dimensional COSY 

spectra where the presence of a cross-peak - indicative of 

coherence transfer - is taken as proof of the existence of 

a scalar coupling. 

We demonstrate that, as a result of multi- 

exponential transverse relaxation, coherence transfer can 

occur between two inequivalent spins that are not scalar 

coupled. Cross-peaks in COSY spectra are shown which arise 

solely from this novel mechanism, and so do no__tt indicate 

the existence of a scalar coupling. Since the use of COSY 

spectra for the analysis of complex spin systems has had 

considerable impact in chemistry and molecular biology, 

the matter of the correct interpretation of cross-peaks is 

one of widespread interest.

WK44 

TWO-DIMENSIONAL POMMIE 13C NMR SPECTRUM EDITING. 

Bruce Coxon 

Center for Analytical Chemistry 

National Bureau of Standards 

Gaithersburg, MD 20899 

The one-dimensional POMMIE (Phase Oscillations to MaxiMlze 

Editing) technique has recently been dev~loped 1,2 as an 

alternative to the DEPT method of spectrum editing. We have 

extended the POMMIE editing method to the two-dimensional domain. 

Our initial studies have focused on 2D POMMIE ~(CH)-resolved 13C 

NMR spectrum editing, using the pulse sequence:- 

~/2(H)-I/2~-~(H)~/2(C)-I/2~-~/2(H)~/2(H,@)z~I/2-~(H)~(C ) - 

i/2~-D-~i/2-acquire 13C, decouple IH, where ~ - IJcH, D is a 

delay (equal to the length of the ~(H) pulse) that was inserted 

to equalize the 13C dephasing and refocusing periods, and the 

pulse pair ~/2(H)~/2(H,~) consists of the multiple quantum 

formation and read pulses, respectively, the latter pulse having 

a variable phase shift 4. 

Automated acquisitions of sets of 2D POMMIE data by three 

different methods (a, b, and c) have been investigated. By use 

of the phase angle set ~ - ~/2, ~/6, and 5~/6, sets of three 2D 

data matrices have been acquired either (a) sequentially, or (b) 

in interleaved fashion, the latter method being designed to 

minimize the effects of sample or spectrometer instability. 

For methods (a) and (b), the 2D POMMIE 13C subspectra were 

computed from the relationships CH - data(~/2), CH 2 - data(~/6) 

data(5~/6), and CH 3 - data(~/6) + data(5~/6) - data(~/2), by 

using the same Pascal software that had been written earlier for 

the purpose of 2D DEPT 13C NMR spectrum editing 3. 

Method (c) involved the direct automated construction of 

the 2D POMMIE 13C subspectra "on the fly", by means of rotating 

phase shifts of the MQ read pulse and the receiver 2. This method 

did not require combination of the 2D data matrices by use of 

software. 

2D POMMIE carbon-proton chemical shift correlated spectrum 

editing has also been implemented by using the sequence:- 

~/2(H)-I~2~-~(H)~/2(C)-I/2J-tl/2-~(C)-~I/2-~/2(H)~/2(H,~ ) - 

i/2~-acquire 13C, decouple IH. - - 

The methods have been applied experimentally to selected 

peptides and carbohydrate derivatives. 

[I] J. M. Bulsing, W. M. Brooks, J. Field, and D. M. Doddrell, 

J. Magn. Reson. 56, 167-173 (1984). 

[2] J. M. Bulsing and D. M. Doddrell, J. Magn. Reson. 61, 197-219 

(1985). 

[3] B. Coxon, J. Magn. Reson. 66, 230-239 (1986).

WK46 

MULTIPLE-ACQUISITION TWO-DIMENSIONAL HOMONUCLEAR 

SHIFT CORRELATION SPECTROSCOPY 

Dieter J. Neyerhoff* and Rudi Nunlist* 

NMR Center 


University of California 

Berkeley, Ca. 94720 

Two-dimensional homonuclear shift correlation spectroscopy 

experiments are very powerful for molecular structure elucidation. 

Experiments such as COSY, delayed COSY, relayed COSY and NOESY are 

routinely used; in order to get reliable information they often 

have to be repeated several times with different parameters. 

Pulse sequences and programs will be given which - similar to 

the CONOESY experiment* - combine such experiments into a single 

pulse sequence. Each dataset obtained this way contains different 

information depending on the stage of magnetization at tha time of 

acquisition. 

Application of these pulse-sequences eliminate the need of 

repeating entire experiments with slightly different parameters 

and thus reduce experimental time and operator interference 

significantly. 

Experimental data will be presented to illustrate the power 

of multiple-acquisition 2D pulse experiments. 

I. Haasnot, C. A. G.; van de Ven, F. J. M.; Hilbers, C. W. J. 

Magn. Res. 1984, 56, 343-349. Gurevich, A. Z.; Barsukov, I. 

L.; Arseniev, A. S.; Bystrov, V. F. J. Magn. Res. 1984, 56, 

471-478.

WK48 

IMPROVED TECHNIQUES FOR THE ACQI//SITION OF TOCSY 

AND CAMELSPIN SPECTRA AND COMPUTER SIMULATIONS 

OF THE TOCSY EXPERIMENT 

Mark Rance 

Department, of Mc~e~ 

R e ~ Ius~t~e of ~ 

10686 North Tm"rey Pines Road 

La Jc~ Califcrni~ 9'2037 

The homonuc]ear HarCmann-Hahn coherence transfer (TOCSY) experiment 

and the r~-frsme NDE (CAMELSPIN) experiment have become very 

im~t ~ far the assignment of proton N MR spectra and for the 

spe~c~r~u of ~ c e ~mstraints for use in structure d~m"u~,~t~rs. For 

optimal results both of these experiments are normally acquired in a manner 

which allows phas~I/ve, alm~'pt/on mode spectz-~ to be obt~ed. 

However, in the most ~ ~ o ~ implemen~ of 1~hese %e~es 

phase anomalies greatly degra~le the quality of the 6pe~r'a. In addit~cm, 

many commercial ~ectrom~ are not ideally suited for the 

hardware demands required for opt~al perfm-mance of these exper~ents. 

We will ~ a novel technique far the ~ 1 ~ ~ of phase anomalies 

which is based an z-fil~ and which can be ea.~y adapted for either the 

TOCSY ¢r the CAMELSPIN experiment and can be readily implemented on 

most. spectrometers. This technique also allows optimal pceit/m~zing of the rf 

during the mixing period in both experiments. Some results will 

also be presented from computer ~im~ of the TO CSY experiment, 

involv'ing the evaluation of various ~ schemes and the determlua.t:m~n of 

optimal experiment parameters for a varie~ af spin sys~ms.

Master Index 

of 

Papers and Posters

Ackerman, J. L ........... MK25 

Adams, R ................. .Wed am 

Aguayo, J ................. WF56 

Albright, M. J ............ .WF60 

Alderman, D. W ......... NIF 19 

Allen, L ................... .MF1 

Allerhand, A .............. WF52 

Anderson, N ........... Mon am 

Andrew, D ............. .Thur am 

Andrew, E. R ............ .WK38 

Anet, F. A. L ............. MF51 

Armitage, H .............. .WK20 

Armitage, I. M ............ WK32 

Auchus, R. J . . . . . . . . . . . . . . WF12 

Bailes, D .................. .WK26 

Balschi, J. A ........... ...WF10 

Bank, Shelton ............ Wed am 

Barbara, T. M ............ MK15 

Barker, P. B .............. WK26 

Baum, J ................. MK01, Sun pm 

Bax, A ..................... WK10, MK23 

Bazzo, R .................. MK43 

Becla, P ................... MF11 

Behar, K. L ............... WF72 

Behling, R. W ............ MF41 

Benesi, A ................. .Wed am 

Bendall, M. R ............ MF57, MF65, 

WF72 

Bermel, W ................ MK37 

Berson, J. A .............. MF29 

Beshah, K ................. WF46, MF11 

Biannuci, A. M ........... Mort am 

Blackband, S ............. .WF56 

Blackledge, M. J ......... WF58 

B15mer, U ................ .WK20 

Bliimich, B ............. WF54, Tue pro, 

Wed am 

Bodenhausen, G ..... .WK42, Tue am 

Boeffel, C ................. Wed am 

Boehmer, J. P ........... MF59, WF76 

Bogusky, M... ........... .WK02 

BoRon, P. H .......... Mon am 

Bonneviot, L .............. WF34 

Borgias, B. A ............ NIK03, Mort am 

Bork, V .................... WF12 

Bowers, C. R ............ MK41 

Bowers, J . . . . . . . . . . . . . . . . . MF31 

Boyd, J . . . . . . . . . . . . . . . . . . . . MK43 

Brandes, R ................ MF45 

Briggs, R. W ............. MF59 

Bronnimann, C. E ....... MF27 

Brown, L. R .............. WK28, MK29 

Brown, S. C .............. WK04 

Boldface Type Indicates Speakers 

Brown, T. R .............. MK27, WF60, 

MF61 

Briischweiler, R .......... Sun pm 

Bryant, D ................. .WK26 

Bryant, R ................. ~IF13, WF14, 

WF42 

Biihlmann, C ............. Sun pm 

Butler, A .................. MF7 

Campbell, G. C ........... WF24 

Carduner, K .............. MF15 

Carter, R. O. HI .......... MF15 

Chang, L.-H .............. WF68 

Chaffield, M. J ............ W-F2 

Chen, D .................... WF32 

Chew, W. M .............. WF68 

Chu, S. C.-K ............. WF10 

Clore, M .................. MK 11, Mon am 

Cockman, M. D .......... WF62 

Cohen, M. S .............. MF61 

Covey, D. F ............... WF12 

Cowburn, D ........... .WK34, Tue am 

Coxon, B ................. .WK44 

Craig, E. C ............... _MK33 

Cross, T. A ............... IvIF47 

Dalvit, C .................. .WK 18 

Danzitz, M ................ MF7 

Darba, P ................... MK29, WK28 

Daugaard, P .............. .WF20 

Davis, D. G ............... MK05 

Dawes, S. B .............. MF25 

De Los Santos, A ........ Mon pm 

de Menorval, L. C ....... .WF8 

Dec, S. F .................. WF18, Tue pm 

Delaglio, F ................ WK30 

Delsuc, M. A ............. .WK30 

Den Hollander, J. A ...... Thur am 

Dixon, T .................. NIF63 

Dobson, C. M ......... MK1, Sun pm, 

Mon am 

Dora, H. C ............... /V[F01 

Drobny, G. P ............. WKS, V~/F22 

Du, L. N .................. MF63 

Dular, T ................... MF73 

Dumoulin, C. L ....... WF64, MF69, 

Tue pm 

Duncan, T. M ............. WF16, W-F34 

Dye, J. L .................. MF25 

Earl, W. L ................ B/IF17 

Eaton, H. L ............... Mon am 

Eckert, H .................. MF07, Wed am 

Eggenberger, U .......... .Tue am 

Ellis, P. D .............. Wed am 

Emerson, S. D ............ WF2 

English, A. D .... ......... WF48

Ernst, R. R ............ Sun pm, Tue pm 

Evans, P. A ............... Sun pm 

Fauth, J.-M ............... Sun pm 

Fesik, S. W ............... WK06, MK07 

Flynn, P. F ................ WK8 

Forbes, J .................. ]VIF31 

FoxaU, D .................. MF65 

Furihata, K ............... MK39 

Gado, M .................. .MF63 

Galvin, M. E ............. .Wed am 

Gamcsik, M. P ........... WK10 

Gampe, R. T ............. .WK6 

Ganapathy, S ............. MF13, WF14 

Garbow, J. R ............. MF21 

Garroway, A. N ......... .MF77 

Garwood, M .............. MF65 

Gemperle, C .............. WK14,Sun pro, 

Tue pm 

Genge, I ................... WK20 

Geoffrion, Y .............. WF66 

Glass, T ................... MF1 

Gleason, K. K ........ MF23, Sun pm 

Glickson, J. D ............ WK10 

Glover, G .............. .Thur am 

Gonen, O ............... MF03, Sun pm 

Gorenstein, D ............. WF44 

Grahn, H .................. WK30 

Grandinetti, P. J . . . . . . . . . . WF4 

Grant, D. M .............. .MF19 

Greenburg, M. M ........ MF29 

Griesinger, C .......... WK14, MK37, 

Sun pm, Tue am, 

Tue pm 

Griffin, R. G .......... MFll, WF46, 

Wed am 

Gronenborn, A. M...Mon am 

Gutowsky, H. S ..... .Wed pm 

Guy, C. A ................ .MF47 

Hallenga, K ............... MF43 

HaUer, G .................. WF34 

Hammel, P. C ............ MF3, Sun pm 

Hanley, C ................. MK1, Sun pm 

Harbison, G. S ....... Wed am 

Hart, H. R. Jr ............. WF64, Tue pm 

Hartzell, C. J ............. .WF22 

Hauksson, J .............. .WF2 

Haw, J. F ................. WF24 

Hengyi, S ................. MK31 

Hermans, W .............. WF36 

Hetherington, H. P ....... WF72 

Hewston, T. A ............ WF30 

Hill, L. E ................. .MF25 

Hiyama, Y ................ .WK16 

Hoch, J. C ............. MK31, Tue am 


Holak, T. A ............... MK13, WF6 

Hornak, J. P .............. WF42 

Hoult, D. I ............. Thur am 

Hseu, T. H ............... MK 19 

Hunter, W. W. Jr ........ MF67 

Husted, C ................ ~ 1 

Jaccard, G ................ .Tue am 

Jakobsen, H. J ............ WF20 

James, T. L ............... WF68, MK3, 

Mon am 

Janakiraman, V .......... .MK25 

Janssen, R ................ .Wed am 

JarreU, H. C ............... WF66 

Jarret, R. M ........... .MF53, Sun pm 

Jarvie, T ................... WF40 

Jelinski, L. W ............ MF41 

Jiang, Y. J ................ MF19 

Job, C ..................... Mon pm 

Johnson, B. A ............ WK32 

Johnson, C. S. Jr ........ WF78 

Johnson, K. M ........... MF43 

Johnston, E ............... MF55 

Jonas, J ................... .WF4 

Jones, C. R ............... WF44 

Jue, T ...................... MK45 

Kang, L ................... .WK40 

Karczmar, G. S ........... WF74 

Kaufmann, S .............. WF54, Tue pm 

Kay, L. E ................. .WF6 

Keams, D. R ............. MF45 

Keller, P.J ................ M1::69 

Kendrick, R. D ........... MF39, Wed am 

Kennedy, S. D ........... MF13, W'F14 

Kentgens, A. P. M ...... .Wed am 

Kessler, H ................ MK37 

Khoury, A ................ .WK2 

Khuen, A ................. .WK20 

King, J. D ................ .Mort pm 

Kintanar, A ............... .WK08 

Kjaer, M ................... MKll, MK31 

Kohlbrenner, W. E ...... MK7 

Kohno, H ................. MF75 

Kolbert, A. C ............. Wed am 

Kopelevich, M ........... _MF51 

Kormos, D. W ............ WF70 

Kreis, R ................... Sun pm 

Kuhns, P ................. 2VIF3, Sun pm 

LaMar, G. N .............. WF02 

Lamb, D. M ............... WF04 

Langer, V .................. WF20 

Laue, E. D ............. .Tue am 

Lawry, T .................. WF74 

Lecomte, J. T. J .......... WF2 

Lee, C ...................... WF32

Lee, K.-B ................. WF2 

Leigh, J. S ................ MF5 

Leighton, P ............... .WK2 

Levitt, M ................ WK22, Tue pro, 

Wed am 

Levy, G. C ............... .WK30 

Limat, D ................... Tue am 

Limbach, H.-H ........... WF26 

Liu, S.-B .................. WF8, MF35 

Loaiza, F .................. WFS0 

Lock, H ................... .WF28, WF38 

LoGrasso, P. V .......... MF47 

Lowe, I. J ................. MF71 

Lu, P ...................... .WK2 

Ludvigsen, S ............. MK31 

Luly, J. R ................. WK6 

Luyten, P. R .......... .Thur am 

Luzar, M ................... WF40 

Maciel, G. E .............. WF18, WF28, 

MF27, WF38, 

Tue pm 

Mack, J. W .............. .WK16 

Madi, Z .................... Sum pm 

Madsen, J. C ............. Sun pm 

Majors, P. D .............. Wed am 

Malikayil, J. A ........... .WK32 

Manders, W. F ........... WF36 

Mao, J ..................... WK38 

Maple, S. R ............... WF52 

Marchetti, P. S ........... .Wed am 

Mareci, T. H .............. WK38, WF62 

Markley, J. L ............. Tue am 

Marshall, A. G ........... MF67, MK33 

Mateescu, G. D .......... MF73 

Matson, G ................. WF74 

Matsui, S .................. MF75 

Mattingly, M .............. WF56 

Matzkanin, G. A ......... Mort pm 

Mayne, C. L .............. MF19 

McCoy, M ................ .WK40 

McDowell, C. A ......... ~[K09 

McGourty, J. L .......... .WF2 

McLennan, I. J ........... .WK10 

McNamara, R ............. WF32 

Meier, B. H ............... MF17 

Meier, B. U ............... Sun pm 

Merrill, R. A .............. MF29 

Metz, K .................... WF76 

Meyerhoff, D. J .......... WK46 

Millar, J. M ............... WF40 

Miller, J. B ............... NIF77 

Mirau, P. A ............ WK12, Tue pm 

Moll, F. III ............... MF47 

Morris, D ................. .Wed am 


Mueller, L ................. WK4 

Muira, H .................. .WF48 

Murphy-Boesch, J ....... WF74 

Narula, S.S ............... WK18 

Navon, G ................. MF41 

Nayeem, A ................ Wed am 

Neiss, T. G ............... MF33, Sun pm 

Nelson, S. J .............. MK27 

Nettesheim, D. G ........ MK21 

Nguyen, K ................ Mon am 

Nicholson, L. K ......... NIF47 

Nicol, A. T ............ .Mon pm 

Nissan, R.A .............. .WF30 

Norris, J. R ............... WK36 

Novic, M .................. Tue am 

Nunlist, R ................. WK46 

O'Neil-Johnson, M ...... MF55 

Ohuchi, M ................ .MK39 

Oldfield, E ................ MF31 

Olejniczak, E. T .......... MK7, MK21, 

WF46 

Opella, S ................... WF32, WK2 

Oschkinat, H ............. .Tue am 

Pardi, A ................... MK17 

Pearson, G. A ............ MK47 

Pearson, R. M ........ Mon pm 

Pekar, J ................... .1VII:z05 

Petrich, M. A ............ MF23, Sun pm 

Peyton, D. H .............. WF2 

Pf~indler,P ................ .Tue am 

Pfenninger, S ............. Sun pm 

Picart, F ................... WK34 

Pines, A ................... WF08, WK24, 

MF35, WF40 

Poulsen, F. M ............ MKll, MK31 

Pratum, T. K ............. .WF22 

Prestegard, J. H ......... WF06, MK13 

Pugmire, R. J ............ MF19 

Quinting, G ............... MF27 

Radda, G. K .............. WF58 

Radloff, C ................ Sun pm 

Ragle, J. L ............. .Wed am 

Raidy, T. E ............... .Wed am 

Raleigh, D. P ............. Wed am 

Ramachandran, R ........ WK28 

Rance, M .................. WK48 

Rath, A. R ................ MF65 

Ream, L ................... Mon pm 

Reid, B. R ................ .WK8 

Reimer, J. A .............. MF23, Sun pm 

Roberts, J. E .......... MF33, Sun pm 

Roberts, M. F ............ .WK22, Tue pm 

Rockway, T .............. .WK6 

Rollwitz, W. L ....... Mon pm

Ronemus, A. D .......... .MF49 

Rooney, W. D ............ MK15 

Root, T .................... WF34 

Ross, B. D ................ WK26 

Rothman, D. L ............ WF72 

Rupprecht, A ............. NIF45 

Rydzy, M .................. WF66 

Ryoo, R .................. .WF8 

Saarinen, T ................ WF78 

Sammon, M. J ........... .MF41 

Santfni, R .................. WF44 

Sarkar, S. K .............. WKI0 

Saunders, M .............. MF53, Sun pm 

Schaefer, J ................ WF12, MF21 

Schenker, K. V .......... .WK24 

Schiksnis, R .............. WK2 

Schmalbrock, P .......... MF67, MF69 

Schmidt, C ................ WF54, Tue pm 

Schoeniger, J ............. WF56 

Sch6nenberger, C ........ Sun pm 

Schussheim, A. E ........ WK34 

Schweiger, A ............. Sun pm 

Scott, K. N ................ WK38 

Seidel, H .................. MF39, Wed am 

Sekihara, K ............... MF75 

Seto, H .................... MK39 

Shan, X ................... MF31 

Shu, A. T ................. MF67 

Shulman, R. G ........... WP'72 

Silver, M .................. WF80 

Simonsen, D. M .......... WF34, WF16 

Singel, D. A .............. MF39 

Sklenkar, V ............... MK23 

Smith, I. C. P ............. WF66 

Smith, W. S ............... WF2 

Soffe, N ................... MK43 

Serensen, O. W ...... .WK14, Sun pm, 

Tue pm 

Souza, S. P ............... WF64, Tue pm 

Spanton, S. G ............ MK35 

Sparks, S. W ............. WK16 

Spiess, H. W ............. WF54, Tue pm, 

Wed am 

Springer, C. S. Jr ....... .MK15, WF10 

Starewicz, P. M .......... WF60 

Stebbins, J. F ............ _MF35 

Stein, H. H ............... .WK6 

Stein, R. S ................ WF36 

Stengle, T. R ............ .MF09 

Stephens, R. L ........... MK35 

Steuemagel, S ............ MK37 

Stewart, P ................. WF32 

St6cklein, W .............. MF39 

Studer, W ................. Sun pm 


Styles, P ................... WF58 

Suter, D ................. WK24,Tue pm 

Suzuki, E.-I .............. ~Ion am 

Swanson, S ............... MF13, WF14 

Szeverenyi, N. M ........ WF80 

Szumowski, J ............. WF42 

Takegoshi, K ............. MK9 

Tang, C. G ................ Tue pm 

Tang, J ..................... WK36 

Thanabal, V ............... WF2 

Thayer, A. M .......... WF40, Wed am 

Theimer, D ................ WF54, Tue pm 

Thoma, W. J .............. WF60, MF61 

Thomas, A ................ Sun pm 

Tijink, E ................... Wed am 

Torchia, D. A ............. WK16 

Tsang, P ................... WF50 

Ugurbil, K ................ MF65 

Vander Hart, D. L ........ WF36 

Veeman, W. S ......... Wed am 

Vogt, V.-D ................ Wed am 

Vold, R. L ................ MF49, WF50 

Vold, R. R ................ MF49, WF50 

Wade, C. G ............... MF55 

Wagner, K ................ MK37 

Walter, T. H .............. MF31 

Wang, C .................. .MK17 

Warren, W. S ......... WK40, MF79, 

Thur am 

Waugh, J. S ........... MF3, Sun pm, 

Tue pm 

Weber, P. L .............. .WK4 

Wef'mg, S ................. WF54, Tue pm 

Wehrle, B ................. WF26 

Weiner, M. W ............ WF74 

Weitekamp, D. P ..... MK41, Thur am 

Westler, W. M ........ Tue am 

White, D ................... WF32 

Whittern, D ............... MK35 

Williams, E. H ........... MF37 

WiUiamson, K. L ....... .MF9 

Wimperis, S .............. .WK42, Tue am 

Wind, R. A ............. WF18, WF28, 

WF38,Tue pm 

Wolff, P. A ............... MFll 

Woolfenden, W. R ...... .MF19 

Wright, P. E .............. WK18 

Wfithrich, K ........... Mort am 

Yamane, T ................ MF41 

Yannoni, C. S ........ .MF39, Wed am 

Yesinowski, J. P .... .Wed am 

Yeung, H. N .............. WF70 

Yu, C ...................... MK19 

Zamir, D .................. .Mt:I 1

Zciglcr, R ................. MF27 

Zhou, N ................... Mort am 

Zicssow, D ............... .WK20 

Zilm, K. W ............... MF29, WF34 

Zon, G .................... Mon am 

Zuiderweg, E. R. P ...... MK21 

Zumbulyadis, N .......... WF38 

Boldface Type Indicates Speakers

List of Attendees 

(registered by March 1, 1987)

Connie L. Ace 

Ethicon Inc. 

Route 22 

Somerville, NJ 08876 

Dorothy A. Adams 

PhilLips Medical Systems 

41Hurd Avenue 

Monroe, CT 06468 

James B. Aguayo 

Johns Hopkins University 

Div. of NMR Research 

310 Taylor 

Baltimore, ND 21205 

Lawrence Atemany 

Mobil Res.& Devet. 

Bittingsport Road 

Paulsboro, NJ 08066 

Witti Ammann 

Varian 

611 Hanson Way 

PaLo ALto, CA 94303 

Karen L. Anderson 


Dept. of Chemistry 

SaLt Lake City, UT 84112 

John A. Anderson 

Univ. of Itt.-Chicago 

P.O. Box 6998-M/C 937 

Chicago, IL 60680 

Frank A.L. Anet 

Univ. of Calif. - LA 

Chem/BiochemDept 

Los AngeLes, CA 90024 

lan M. Armitage 


Dept Mot Biophy/Biochem 

P.O. Box 3333 


Cheryl H. Arrowsmith 

Stanford Magnetic Resonanc 

Stanford University 

Stanford, CA 94305-5055 

Jerome L. Ackerman 

Mass Gent Hospital 

NMR Facility Baker 2 

Dept. of Radiology 

Boston, NA 02114 

Bruce R. Adams 

University of Wisconsin 

1101 University Avenue 

Madison, WI 53706 

Michael J. Atbright 


186WoodAve. South 

lsetin, NJ 08830 

Brian D. Attore 

Sick ChiLd. Hosp. 

88 ELm St., 5th fLr 

Toronto,Ont.Canada 

Karl R. Amundson 

Univ. Cal. - BerkeLey 

Dept. of Chem. Eng. 

Berkeley, CA94720 

StanLey E. Anderson 

Westmont CoLlege 


Santa Barbara, CA 93108 

WiLLiam R. Anderson 


S.G. Mudd Btdg #6 

BethLehem, PA 18015 

Eric. V. AnsLyn 

Cat Tech 


Robert D. Armstrong 

GE NMR Instruments 

20 TechnoLogy Pkwy. 

Suite380 

Norcross, GA 30092 

Dennis J. Ashworth 

Stauffer Chemical 

1200 S. 47th Street 

Richmond, CA 94804 

Gato Acosta 

Diasonics, Inc. 

533 Cabot Road 


Robert E. Addleman 

Indiana University 


Bloomington, IN 47405 

Donald W. Alderman 


Chemistry Dept. 

Salt Lake City, UT 84112 

John D. Attman 

Univ.of CaLifornia 

Dept. Pharm. Chem. 


A.M.(Andy) Anderson 

Witmad GLass Co., Inc. 

1506Uppinghan Rd. 

Thousand Oaks, CA 91360 

Niets H. Anderson 

University of Washington 



D. Andreu 

See abstract 

Byron H. Arison 

Merck & Co. 

P.O.Box 2000 

Rahway, NJ 07065 

Henry C. Arndt 

Miles Laboratory 

1129 Myrtle St. 

Elkhart, IN 46514 

Hector Avram 

Oiasonics, Inc. 

533 Cabot Rd 

San Franciso, CA 94080

David Axe[son 

EMR-CoaL Research Labs 

Canmet/Crt PO Bag 1280 

Devon ALberta 

Canada TOC lEO 

ALex D. Bain 

Bruker Spectrospin Ltd 

555 Steele Ave. E 

Mitton,Ont.Canada L9T 1Y6 

Lairna Battusis 

Varian 


Fort Col[ins, CO 80525 

Thomas M. Barbara 

SUNY - Stony Brook 

Dept of Chemistry 

Stony Brook, NY 11794 

Vtadimir J. Basus 


School of Pharmacy 

BOX 0446 


Jean Baum 

Oxford University 

Inorganic Chem. Lab 

South Parks Rd. 

Oxford, England OX13QR 

Ad Bax 

Natt[ ]nst of Health 

gtdg 2 Rm 109 

Bethesda, ND 20892 

William H. Bearden 

JEOL USA ]NC. 

11 Dearborn Road 

Peabody, NA 01960 

Larry Becket 

General Chemical Corp. 

344 W.Oenesee St. 


John H. Begemann 

New Methods Research Inc. 

719 E. Genesee St. 


Mary S. Bailey 

Univ. of Cincinnati 

Col Med Dept Ant/Celt Bio. 

2.31 Bethesda Ave. 

Cincinnati, OH 45229 

John H. Batdo 


255 Fourier Ave. 

Fremont, CA 94536 

Shetton Bank 

Univ of South Carolina 

MRL 

Columbia, SC 29208 

Peter B. Barker 

HMRI 

10 Pico Street 


Lyrme S. Batchetder 


611Hansen Way 

Pato Afro, CA 94303 

Mary W. Baum 

Princeton University 


Princeton, NJ 08544 

Renzo Bazzo 


Dept. of Biochem 

Oxford, Eng., UK OX1 3QR 

gittiarn T. Beaudry 

Chem. Res. & Dev. Ctr. 

SMCCR-RSC-P/Beaudry 

Abrdn Prv.Grd., MD 21010-5 

ALvin J. Beeter 

I.E. DUPONT de NEMOURS 

Wilmington, DE 19898 

Ronatd Behting 

AT&T BELL LABS 

Room 1C-432 

600 Mountain Ave. 


David B. Bailey 

USI Chemical 

1275 Section Rd. 


James A. Batshi 

Harvard Medical School 

NMR Lab 

221Longwood Ave. 

Boston, NA 02115 

Oebra L. Banvitte 

UCSF 

Dept. of Pharmaceut. Chem. 


Victor J. Bartuska 

Chemagnetics 

209 Commerce Dr. 


Lorenz J. Bauer 

Allied Signal 

50 E. ALgonquin Rd. 

Des Ptaines, lL 60017 

Karen P. Baum 

Univ. of Ca[if. 

ChemDept. 


John M. Beate 

Ohio State University 


120 W. 18th Ave. 


Edwin D. Becker 

NIH 

Btdg l/Rm 118 

Bethesda, MD 20892 

James W. Beery 

Sandoz Crop Protect.Corp 

]41E. Ohio Street, 

Mail Stop 5120 

Chicago, lL 60611 

M. Robin BendaLt 

Varian 

Griffith Univ Sch Sci. 

Nathan, Queensland 

Australia 4111

Alan Benesi 

Penn State University 


NNR Lab 

University Park, PA 16802 

Benedict W. Bergerter 



225 Prospect St PO Box 666 


Nichae[ A. Bernstein 

Nerck Frosst Canada 

PO BOX 1005 

Pointe Ctair-Oorvat, 

Quebec/Canada H9/R 4P8 

Norman S. Bhacca 


Louisiana State Univ. 

Baton Rouge, LA 70803 

Harriet Bible 

Sargent Welch 

9012 Nango Ave. 

Norton Grove, IL 60053 

Karen K. Bittner 

Raychem Corp. 

300 Constitution Ave. 

Menlo, CA 94025 

C. Scott Btackwett 

Union Carbide Tech Ctr. 

Old Sa~nitt River R. 

Tarrytoun, NY 10591 

Michael J. Bogusky 

University of Penn. 

ChemDept. 

Philadelphia, PA 19104 

Manju S. Bonsatt 

Indian lnst of Science 

Bangatore, India 560012 

Richard Borders 

Kimberly Clark 

Btdg 4001408 

1600 HotcombBridge 

Roswetl, GA 30076 

Mabry Benson 

USDA West Reg Res Ctr 

800 Buchanan St. 

Albany, CA 94710 

Bruce 1. Berkoff 

University California 

Biophysics Group 

22 Gitman Halt 

Berkeley, CA 96720 

Richard D. Bertrand 

University of Colorado 

Dept. of Chem. 

PO BOX 7150 Austin Bluffs 

Cot. Sprgs, CO 80933-7150 

Anna Maria Bianucci 

UCAL SF 

Dept. of Pharm. Chem. 

513 Damassus Ave. 


Anthony Bietecki 

MIT Nat'[ Nag Lab 

Btdg NW14 

Cambridge, HA 02139 

Stephen J. Blackband 

Johns Hopkins Univ. 

School of Med. 

720 Rutland Ave. 

Baltimore, MD 21205 

Bernhard Btuemich 

MAX PLANC-INST POLM CHUNG 

Postfach 3148 

D-6500 

Mainz, Germany 

Lizann Botinger 

Univ. of Penn. 

Biochem/Biophys 


Jo-Anne K. Bonstee[ 

DuPont Exper Sta. 

PPD E269 

gitmington, DE 19898 

Phittip Borer 

Syracuse University 

1117 gestcott St. 


Jack A. Berdasco 

Potym. Mat'| Res. Gr. 

574 Btdg/Dou Chemical Co. 

Midland, Ri 48667 

Wotfgard Bermet 

Bruker Instruments 

Manning Park 

Bitterica, HA 01821 

Kebecle Beshah 

Francis Bitter Nat't. 

Nagnet. Lab 

NW 14-5107/NIT 


Roy Bible 

G.D. Searte & Co. 

6901Searte Pkwy 

Skokie, ]L 60077 

Donald C. Bishop 

Chemagnetics, inc. 



Martin J. Blacktedge 

Univ. of Oxford 

MRC Biomed NRR Facility 

John Radcliffe Hospital 

Oxford/UK 

Geoffrey Bodenhausen 

Univ. of Lausanne 

Inst de Chimie Organique 

Rue de ta Barre 2 

1005 Lausanne, Switz 

Philip H. Botton 

Wesleyan University 


Niddteton, CT 06457 

Babut Borah 

Norwich Eaton Pharm. 

I~D Box 191 

Woods Corners, 

Norwich, NY 13815 

Brandan A. Borgias 

Univ. of Calif.- SF 


San Francisco, CA 94163

Vincent P. Bork 

Washington Univ. 


St. Louis, NO 63130 

Akset A. Bothner-By 

Carnegie-Relton Univ. 

Dept. of Chem 

Pittsburgh, PA 15213 

C. Russell Bowers 

Cattech 

Arthur Amos Noyes Lab 


Raymond J. Brambitta 

ALLied-Signal 

Morristown, NJ 07960 

Anita Brandotini 

Mobil Chem. Co. RgO 

PO Bx 240 

Edison, HJ 08818 

Christian Brevard 


Ranning Park 

Bitterica, NA 01821 

Jacques Briand 

Univ British Columbia 

Dept Chem2036 Rain Halt 

Vancouvera Brt. Col. 

Canada V6T 1Y6 

Chuck E. Bronniman 

CSU Reginat NNR Facility 

Dept of Chem 



Bernadette A. Brown 

IBR 

166 Hillside Ave. 

Riveredge, NJ 07661 

Stephen C. Brown 

Smith Ktine & French Labs 

709 Suedetand Rd. 

Swedetand, PA 19479 

Rarie Borzo 

Hoechst-Cetanese 

86Norris Ave. 

Summit, NJ 07901 

James H. Bourett 

Plant Celt Research Inst. 

1548 Brentwoed Ct. 

Walnut Creek, CA 94595 

Jonathan Boyd 


Dept. of Biochem. 


Oxford, England, UK 

Malcolm R. Brarnwett 


2880 Zanker Rd. Ste 106 

Jan Jose, CA 95134 

Steve Brandt 

Chemical Dynamics Corp. 

3001 Hadley Rd. 

S. Plainfield, NJ 07080 

Wallace S. Brey 

Univ. of FLorida 

ChemDept 

Gainesvitte, FL 32611 

Richard W. Briggs 

Hilton Hershey Ned Ctr 

Dept. of Radiology 

PO Box 850 

Hershey, PA 17033 

Arthur L. Brooke 

Oxford Magnet Technology 

Eynsham, Oxforshire 

England, UK OX8 1BP 

Leo D. Brown 

NRR Instruments 



Truman R. Brown 

Fox Chase Cancer Center 

7701Burhotme Ave. 


Richaet D. Boska 

V.A. Medical Ctr.-S.F. 

RRS Lab 

4150 CLement St. 


John L. Bowers 

Univ. of ILLinois 

Box 18-1Noyes Lab 

Urbana, IL 61801 

Joel C. Bradley 

Cambridge Isotope Lab. 

20 Coemerce Way 

Woburn, NA 01801 

Rotf Brandes 

Univ. of California 

San Diego 

Dept. of ChemB-014 

La Jotta, CA 92093 

Gerald T. Bratt 

University of Rinnesota 

Biochem. Dept. 

435 Deteware St. SE 

HinneapoLis, RN 55455 

William Brey 

Univ. Texas/Hed/Radiot. 

UT Health Center - Houston 

6431Fannin 

Houston, TX 77030 

Hichette S. Broido 

Hunter College Chem Dept. 

695 Park Ave. 

Neu York, NY 10021 

Etwood E. Brooks 

Univ. of Cincinnati 

Chem Dept ML172 


Ronatd D. Brown 

Merck & Co. 

PO Box 62000 R80M-113 


Larry R. Brown 

Australia Nat't Univ. 

RES School of Chem 

Canberra, A.C.T. 

Austral ia 2601

Hark S. Brown 

Yale School of Hed. 

Dept. of Diag. Rad. 

333 Cedar St CB58 

Neu Haven, CT 06511 

Hartha Bruch 

DuPont Expermtt Station 

Polymer Preducts Dept. 


Thomas E. Butt 

FDA/Btdg 29/Rm530 

8800 Rockvitte Pike 

Bethesda, HI) 20892 

Douglas P. Burum 


Hanning Park 


Gordon C. Campbell, Jr. 

Texas AgN 

Dopt. of Chemistry 

cortege Station, TX 7-/843 

James L. Carotan 

Natorac Cryogenics Corp 

837 Arnold Dr Ste. 600 

Hartinez, CA 94553 

Louis G. Carreiro 

Army Rat Tech Lab 

SLCRT-OHN Arsenal St. 

Watertown, HA 02172 

Toni L. Ceckter 

Univ Rochester Red Ctr 

Biophysics Dept. 


Lawrence Chan 

Univ Colorado 

Sch of Med. 

Box C280 4200 E 9th St 

Denver, CO 80262 

Hsu Chang 


533 Cabot Rd. 

S. San Francisco, CA 94080 

Rodney D. Brown Ill 

lBN Research Labs 

PO Box 218 

Yorktown Hgts., NY 10598 

Robert G. Bryant 

Univ Rochester Ned Ctr 

Biophysics Dept. 


Steven A. Bumgardner 

Chen~gnetics, Inc. 

208 Con~rce Dr. 


C. Allen Bush 

lttinois Inst. Tech 



Steve Caravaja[ 

Proctor & Gant~te 

5299 Spring Grove Ave 


Thomas A. Carpenter 

Cambridge Univ. 

Lab Ned Che~n/Ctin Sch 

Aclclen Brooke's Hosp. 

Canbridge, UK 

Lewis W. Cary 

GE NNR Instruments 



V. P. Chacko 

Johns Hopkins fled Inst 

110MRI, Dopt Rad. 

600 Wolfe St. 

Baltimore,, ND 21205 

Tze-Ning Chan 

Schering Corp. 

60 Orange St. 

Bloomfield, NJ 07003 

Shoumo Chang 


Chemistry Dept 

lrvine, CA 92717 

Sydney K. Brownstein 

Nat't Res Council Canada 

Chemistry Div. 

Ottawa,Ont,Canada K1A OR9 

Edward Bubienko 

G.E. Red Sys. Group 


Freemont, CA 92439 

Louet[ J. Burnett 

San Diego State University 

Physics Oopt. 

San Diego, CA 92119 

R. Andrew Byrd 

BiD LaWCtr Drugs/Biol. 

NIH Btdg 29-432 


Keith R. Carduner 

Ford Notor Co. 

Research Staff 

Dearborn, M! 48121 

Allan Carr 

Anderson Urot.Assoc. 

218 E. Calhoun St. 

Anderson, SC 29621 

Nichaet Cassidy 

Oxford Instruments 

3A Alfred Circle 

Bedford, HA 01730 

Linda D. Chadwick 

Siemens Ned. Syst. 

186 Woo(] Ave S. 

Isetin, NJ 08830 

S. Chandrasekar 


Georgia State Univ. 

Atlanta, ~ 30303 

Jih-Wen Chang 

Univ. Cal.-Berkeley 

Mail Stp 11-B85 

Dept of Chem 

Berkeley, CA 94720

Lydia L. Chang 

Stauffer Chemical Co. 

1200 S. 47th St. 


Hark A. Chaykovsky 


Manning Park 

Bitlerica, MA 01821 

Benjamin Chen 

YaLe Univ. Sch Ned 

Dept Diag. Rad 

333 Cedar St. 

HeM Haven, CT 06510 

N. g. Cheng 

HercuLes Inc. 

Research Center 

WiLmington, DE 19894 

Kenner A. Christensen 

Univ of Arizona 

ChemDept 

Tuscon, AZ 85721 

John Chung 

Univ of ILLinois 

Box 30 Noyes Lab 

505 S. Nathews 


Hike N. Ctingan 

Doty Scientific Inc. 

600 Ctemson Rd. 

CoLumbia, SC 29223 

Robert Codrington 


611 Nansen gay 

Pato ALto, CA 94303 

Lawrence D. Cotebrook 

Concordia Univ/Chem 

1455 deMaissoneuve BL W 

Nontreat,Oue 

Canada H3G 1N8 

Chuck Connor 

Dept of Chem 

Univ of Cat 

BerkeLey, CA 94720 

Hark D. Chatfietd 

Univ. of CaLif.,Davis 

ChemDept 

Davis, CA 95616 

WaLter J. Chazin 

Res lnst Scripps CLinic 

NB-21103 

10666 N. Torrey Pine Rd. 


Deng-Ywan Chen 

Univ of Penn. 

Dept of Chem 

PhiLadeLphia, PA 19104 

Peter Cheung 

PhiLLips PetroLeum 

347A Petro. Lab 

PhiLLips Res. Ctr. 

Barttesvilte, OK 74004 

Simon C. Chu 

Univ. of Cat Davis 

NHR FaciLity 


Theodore C. Ctaiborne 

Hedrad Inc. 

271 Kappa Hanor Dr. 


David N. Cochran 

Ayerst Labs Research 

CH 8000 


Scott g. Coffin 

RockefeLler Univ. 

1230 York Ave. 

New York, NY 10021-6399 

Kimberty L. Cotson 

YaLe Univ.Ned Sch 

Dept of Pharm. 

333 Cedar St 


Noodrow N. Conover 

GE NHR instruments 



Nariann J. Chatfietd 

Univ of CaL.-Davis 

ChemDept 


Brad F. Chemetka 

Univ of Cat BerkeLey 

Dept of Chem Eng. 


Doris Cheng 

Exxon Chemical Co. 

PO Box 45 

Linden, NJ 07036 

Gwendotyn N. Chmurny 

NCi Frederick Cancer 

Research Center 

PO Box B 

Frederick, MD 21701 

l-Ssuer Chuang 

Chemistry Dept Bx42 

CoLorado State Univ. 

Ft Cottins, CO 80523 

Niger J. Ctayden 

ICI PLC, lnt'l Nat't Ctr 

P 0 Box 90 

Nitton,Hiddtesbrough 

CLeveLand,England TS6 8JE 

Hichaet D. Cockman 

Univ of Fla. 

Box 71 

Leigh HaLt 

Gainesvilte, FL 32611 

Hetga J. Cohen 

Univ. of South CaroLina 

Chem Dept NNR Lab 


Thomas Connick 

Dory Scientific 

600 Ctemson Rd 


Frank Contratto 

Varian Assoc. 

505 Jutie Rivers Rd. 

Sugar Land, TX 77478

Michael Cooper 

Lockheed MSC 0/48-92 

1111 Lockheed Way 

B/195B 

Sunnwate, CA 94089-3504 

Paul Cope 

Witmad Glass Co. 

Route 40 & Oak Rd. 

Buena, NJ 08310 

Charles E. Cottrelt 

Ohio State Univ. 

CCIC 


CoLumbus, OH 43210 

Edward Craig 


Dept of Chem. 

120 W 18th Ave 

CoLumbus, OH 43210-1173 

Roger W. Crecety 

Univ of Delaware 

ChemDept. 

Newark, DE 19716 

Richard C. Crosby 

Texas AgN 

Dept. Chem. 

cortege Station, TX 77843 

Joseph C. Crowtey 

Lockheed Misstes/Spece 

3251 Hanover St 

8204/09350 

Pato ALto, CA 94304-1191 

John D. Cutnett 

So. Illinois Univ. 

Physics Dept. 

Carbondate, IL 62901-4401 

David C. Oatgarno 

American Cyanamid 

PO Box 400 


Prashanth Darba 

Univ Wisconsin/Madison 

Dept of Biochem 

420 Henry Matt 


James W. Cooper 

IBM Instruments 

PO Box 8332 

Danbury, CT 06813 

Chris Coretsopeutos 

Univ. of ILLinois 

Dept of Chem 



David Couburn 

RockefeLLer Univ. 


Box 299 

New York, NY 10021-6399 

Ray Crandatl 

Xerox Corp 

800 Phillips Rd. 

Webster, NY 14580 

Robert Creekmore 

FMC Corp. 

PO Box 8 


Timothy A. Cross 

FLorida St. Univ. 

Chem Dept 

Tattahassee, FL 32306 

Sean A. Curran 

Monsanto Co. 

730 Worcester St. 

SpringfieLd, MA 01151 

Dana Andre D'Avignon 


Campus Box 1134 


Jerry L. DaLLas 




Darrell R. Davis 

Univ of Utah 



Walter G. Copan 

Lubrizot Corp 

29400 Lakeland Btvd 

Wicktiffe, OH 44092 

Mary Lou Cotter 

Ortho Pharm. 

Route 202 

Raritan, NJ 08869-0602 

Bruce Coxon 

Nat'[ Bur of Stds 

Chemistry BLdg A361 

Gaithersburg, HI) 20899 

Eaten Crecety 

Brandywine Res. Labs 

226 W Park PLace 


Robert M. Crosby 

M-R Resourses Inc. 

262 Lakeshore Dr. 

PO Box 642 

Ashburnham, IdA 01430 

Michael Crowtey 

Harper Grace Hospitat 

NMR Center 

Detroit, M! 48201 

Janet C. Curtis 

Univ of Utah 


SaLt Lake City, UT 84112 

Josef Oadok 

Carnegie MeLton Univ. 


4400 Fifth Ave. 


Neat Dando 

ALcoa 

Anal Chem Tech Ctr 

ALcoa Center, PA 15046 

Detphine Davis 

Univ Cat/Santa Barbara 

Dept of Chem 

Santa Barbara, CA 93106

Nicotette Davis 

View Engineering 

1656 Emeric Ave. 

Simi Valley, CA 03065 

Steven F. Dec 

Colorado St. Univ. 

Dept of Chem 


Alan J. Deese 

Genera[ Electric 

Ned. Systems Group 



E. James Detikatny 

Univ of British Columbia 


Vancouver/BC/Canada V6T1Y6 

Peter C. Demou 

Yate University 

ChemDept 

PO Box 6666 


Jeffrey S. deRopp 

Univ of Cat-Davis 

NMR Facility 


Heather Dettman 

University of Ottawa 

Dept of Chem 

Ottawa 

Ontario/Canada K1N9B4 

Lisa M. DiMichete 

Merck & Co., Inc. 

PO Box 2000 

Btdg 801Rm 210 


Thomas Dixon 

Emory Univ. 

Radiology Dept. 

412 Woodruff Hem.Bldg. 

Atlanta, GA 30322 

Peter J. Domai[le 

DuPont Exp. Station 


Donald G. Davis 

NIEHS 

Lab Note. Biophycs. 

PO Box 12233 

Research Tri. Pk, NC 27709 

Rona[d L. Dechene 

Auburn lnt't. IMR Div. 

Eight Electronics Ave. 

Danvers Industrial Pk. 

Danvers, HA 01923 

Frank Oetagtio 



Syracuse, HY 13210 

Marc Detsuc 

Syracuse Univ. 

305 Bowne Hat[ 


Christopher E. Dempsey 



South Park Rd 

Oxford/England, UK OXl 3QU 

Christian Detettier 

University of Ottawa 


Ottawa/Canada K1N9B4 

Lisa A. Deuring 

Varian Assosciates 

255 Fourier Ave 


Bob DiPasquate 

JEOL USA Inc 

11 Dearborn Rd. 

Peabody, HA 01960 

Chris N. Dobson 

Oxford Univ. 

Oept of ]norg. Chem. 

South Parks Rd 

Oxford England, UK OX1 30R 

Robert Lee Domenick 

Stanford Nag. Res. Lab. 



William Dawson 

Canmet, Energ.Res.Lab. 

555 Booth Street 

Ottawa/ 

Ontario/Canada KIA OG1 

James J. Dechter 

Arco Oil & Gas 

PRC-1C17 

2300 W. Piano Pkwy 

Piano, TX 75075 

John L. DeLayre 

Tecmag Inc. 

6006 Bettaire Blvd. 

Ste. 118 


Louis C. DeNenorvat 

Univ of Cal.-Berkeley 

Dept of Chem. 


Lawrence W. Dennis 

Exxon Res & Eng 

PO Box 4255 

Baytown, TX 77522-4255 

George Detre 

SRI International 

333 Ravenswood Dr. 

Menlo Park, CA 94025 

Susan L. Dexheimer 

Laurence Berke[ey Lab 


Joseph A. DiVerdi 

Chemagnetics Inc. 


Ft. Cottins, CO 80524 

Jack Ooherty 




Harry C. Oorn 

vPI 


Blacksburg, VA 24061

F. David Doty 




Daniel R. Draney 

American Cyanamid Co. 

1937 W. Main St. 

Stamford, CT 06904-0060 

Susan Oruckman 

E.R. Squibb 

PO Box 4000 


Haureen A. Duffy 

Can~oridge Isotope Labs 

20 Commerce Way 

Woburn, HA 01801 

R. William Dunlap 

Amoco Research Center 

PO Box 400 

Napervitte, IL 60566 

Cecil Dybowski 

University of Delaware 


Neward, DE 19716 

Thomas A. Early 


255 Fourier Way 


William M. Egan 

FDA Biophys.lab 

Ctr Drugs & Biologies 

gethesda, MD 20892 

Henry Eisenson 

Sciteq Electronics 

8401Aero Drive 


John Eng 

Princeton Univ. 



Judy M. Dory 




Edward A. Dratz 

Montana State Univ. 

Dept of Chem. 

Bozeman, MT 59717 

George R. Dubay 

Duke University 


P.M. Gross Chem Labs 

Durham, NC 27706 

Charles L. Dumoutin 

Genera[ Electric Co. 

Res. & Devet. Ctr. 

PO Box 8 KI-NMR 

Schenectady, NY 12301 

Theresa S. Dunne 

Lederte Labs 

Middletown Rd. 658/320 

Pearl River, NY 10965 

Thomas M. Eads 

Kraft Inc., Tech Ctr. 

801Waukegan Rd. 

Gtenview, IL 60025 

Het[mut Eckert 

Cat. Tech. 


Mail 164-30 


Thomas F. Egan 

Tecmag 

6006 BetAir Blvd. 


Paul D. Ellis 

Univ of So.Carolina 



Cart E. Engteman 




Montee A. Doverspike 

Naval Res. Lab. 

Code 6120 

4555 Overtook Ave., SU 


Gary Drol0ny 


Univ. of Washington 


Eliot W. Dudley 




T. Michael Duncan 

AT&T Belt Labs 

6E-318 

Murray Hilt, NJ 07974-2070 

Lois J. Durham 


ChemOept. 


William L. Earl 

Los Atames Nat't Lab. 

Mail Stop C345 

Los Atames, NM 87545 

Richard R. Eckman 

Exxon Chemical 

5200 Bayway Dr. 

Baytown, TX 77520 

Keigi Eguchi 

JEOL USA [NC 

1418 Nakagami 

Akishima, 196 

Tokyo Japan 

Steven Donald Emerson 


Chem. Dept. 


ALan D. English 

DuPont Exp. Station 

Central Res & Devel. 

Wilmington, DE 19898

Raut G. Enriquez 

]nstituto De Ouimica 

Univ. Nacionat Autonoma 

Circuito Exterior 

Ciudad Univer., MX 04510 

C. Anderson Evans 

Berlex Laboratories Inc. 

110 E. Hanover Ave. 

Cedar Knolls, NJ 07927 

Mary Fabry 

Einstein Col. Med. 

1300 Morris Park Ave. 

Bronx, NY 10461 

Rod Fartee 

DuPont Central Res. 

E328/126 


Thomas C. Farrar 

Univ of Wisconsin 


Madison, Wl 53706 

Jeffrey R. Fitzsimmons 

Shands Hosp. JHMHC 

Dept of Radiology 

Gainesvilte, FL 32601 

Peter F. Ftynn 


Dept of Chemistry BG-IO 


Peter Forster 

University of Otkahoma 


Norman, OK 73019 

Stephen Freetand 

Chemagnetics 



Alan J. Freyer 

Penn State Univ 

152 Davey Lab Chem Dept 

University Park, PA 16802 

George Entzminger 

Doty Scientific 

600 Clemson Rd. 


Jerenn/ R. Everett 

Beecham Pharmaceuticals 

Brockham Park 

Betchworth, 

Surrey, UK RH3 7AJ 

Paul E. Fagerness 

Upjohn/Product Control II 

7832-259-12 

Portage Road 

Kalamazoo, MI 49001 

Bruce W. Farnum 

Certified Tech Corp. 

7404 Washington Ave. So. 

Minneapolis, MR 55344 

Raymond Ferguson 

Condux, Inc. 

300 Whitby Dr. 


William W. Fleming 

IBM Almaden Res K91/801 

650 Harry Road 

San Jose', CA 95120-6099 

Jeffrey Forbes 

Univ. of illinois 

Noyes Lab Box 42-1 

505 S. Mathews 


Natalie Foster 

Lehigh Univ. 


Mudd Btdg #6 


Dominique Freeman 

G E Red Syst 



Richard M. Fronko 

Naval Research Lab 

Code 6122 

Washington, 0C 20375-5000 

Richard R. Ernst 

ETH Zurich 

Lab. Physikalische Chemie 

ETH-Zentrum 

Zurich Switzerland 8092 

Edward L. Ezett 

UT Medical Branch 

Galveston, TX 77550 

Teresa Fan 

Univ.Calif-Davis 

NMR Facility 


Sylvia A. Farnum 

3N Corp. 

Spec.Chem Lab 

Bldg 236-2B-11, 3M Ctr. 

St. Paul, MN 55144-1000 

Stephen W. Fesik 

Abbott Laboratories 

D-47G AP9 

Abbott Park, IL 60064 

Timothy Flood 

PPG 

PO Box 31 

Barberton, OH 44203 

Charles E. Forbes 

Celanese Research Co. 

86Morris Ave 


David Foxatt 


1120 Auburn Street 


Michael H. Frey 

JEOL USA INC 



David Fry 

Hoffman-LaRoche, Inc. 

Dept of Physical Chem. 

Nuttey, NJ 07110

James S. Frye 

Colorado State Univ 

Dept of Chem 

Ft ColLins, CO 80523 

Bing N. Fung 

Univ of Otkahorna 


Norman, OK 73019 

Nichaet Fuson 

Wabash CoLlege 

Dept of Chem 

Crawfordsvitte, IN 47933 

Michael Gamcsik 

John Hopkins Univ. 

720 RutLand Ave. 

BaLtimore, HD 21205 

Joel R. Garbow 

Honsanto Co. 

Life Sciences, NHR Ctr 

700 ChesterfieLd Vlg Pkb~y 


Hichae[ Garwood 

Univ of Ninnesota 

Gray Freshwater 

Biological Institute 

Navarre, HN 55392 

John H. Geckte 

Bruker Instrument 

Manning Park 


Robert T. Gempe Jr. 

Abbott Labs AP9 

Pharm. Discv. Div 

RMR Research Group 

Abbott Park, IL 6006/+ 

John T. Gerig 

Univ of CaLifornia 



Athot[ A. Gibson 

gatorac Cryogenics 

837 Arnold Dr. Ste.600 

Nartinez, CA 94553 

Toshimichi Fujiuara 

JEOL Ltd. 

Biomet Lab 

1418 Nakagami-Akishirna 

Tokyo/Japan 196 

Kazuo Furihata 

Univ of Tokyo 

lnst of AppLied Biology 

Bunk You-Ku 

Tokyo Japan 

Colin A. Fyfe 

University of GueLph 

Guelph 

Ontario Canada N1G 2U1 

Zhehong Gan 



Janice Kotes Garde 

Nonsanto Co. 

800 N. Lindberg Btvd 

St Louis, NO 63166 

Nancy K. Geananget 

Univ of Houston 


4800 Calhoun 


Thomas E. Gedris 

Florida State Univ. 


Tattahassee, FL 32306 

Yves Geoffrion 

See abstract 

Bernard C. Gerstein 

Iowa State University 

229 Spedding 

Ames, IA 50010 

Dara E. Gilbert 

UCLA 

Dept of Chem& Biochem 

405 Hitgard Ave. 


Eiichi Fukushima 

Lovetace Nedicat Found. 

2425 Ridgecrest Dr. SE 

Atbuciuerque, NH 87108 

George T. Furst 

Univ of Penn 


PhiLadelphia, PA 1910/+ 

Robert A. Gate 

N. R. Resourses 

PO Box 642 


Ashburnham, HA 01430 

ALbert R. Garbsr 

Univ of So CaroLina 

ChemOept 


AlLen N. Garroway 

Naval Research Labs 

Cede 6122 


Russett A. Geanange[ 

Univ of Houston 


4800 CaLhoun 


Leslie T. Gelbeum 

Georgia Tech 

Dept of Applied Biotogy 

AtLanta, GA 30332 

Walter V. Gerasirnowicz 

USDA - ERRC 

600 E Nermaid Lane 


Paul J. Oiammatteo 

Texaco Inc. 

PO Box 509 

Beacon, NY 12508 

Russell W. Gittis 

The Upjohn Co. 

1140-230-2 

7171 Portage Rd. 

Kalamazoo, HI 49001

Peter S. Given 

Nabisco Brands 

100 DeForest Ave. 

PO Box 1941 

E. Hanover, NJ 07936 

Karen Gteason 

Univ of California 


Berketey, CA 94720 

G. Gtover 

See abstract 

Wench/ Gotdberg 

Merck Isotopes 

PO Box 2000 


Ricardo R. Gonzatez-Mendez 

Resonex Inc. 

720 Patomar Ave. 

Sunnyvate, CA 94086 

Warren J. Goux 

Univ of Texas -Dattas 


PO Box 688 

Dattas, TX 75080 

David M. Grant 


University Utah 

Satt Lake City, UT 84112 

Christian Griesinger 

Eth-Zurich Phy Chem Lab 

Eth-Zentrum 

CH-8092 

Zurich, Switzerland 

Chartes M. Grisham 

Univ of Virginia 


Chartottesvitte, VA 22901 

Terry W. Gultion 




Jay A. Gtaset 

Univ of Connecticut 

Oept of Biochemistry 

Hearth Center 

Farmington, CT 06032 

James W. Gteeson 

Mobit Res. & Oevet. 

PO Box 819047 

Dattas, TX 75381 

Gian C. Gobbi 

Dow Chemicat (Canada) 

PO Box 3030 

Vidat St.S. Sarnia, 

Ontario, Canada NTT 7M1 

Nina C. Gonetta 

ciba Geigy 

556 Morris Ave. 


Paut R. Gootey 


7171 Portage Rd. 

7832-259-12 

Katamazoo, HI 49001 

David W. Graden 

Ortho Pharm. Corp. 

Route 202 

Raritan, NJ 08869 

Peter Grant 


505 Ju[ie Rivers Road 

Sugar Land, TX 77478 

Robert G. Griffin 

Nationat Magnet Lab 

NW14-5113 MIT 

77Massachusetts Ave. 


Stephen H. Grode 


1140-250-2 


Wei Guo 

Univ Missouri-Columbia 

Dept of Chem. 

Cotumbia, MO 65211 

Tho(nas E. Grass 

VPI 


Btacksburg, VA 24061 

Jerry D. Gtickson 

Johns Hopkins Hospitat 

Sch of Med/Dept of Rad. 

Taytor Btdg Rm 310 

Battirnore, MD 21205 

Laurence A. Goff 

ICI Americas, Inc. 

Witmington, DE 19897 

Oded Gonen 

MIT 

RM-6-133 


Myra Gordon 

Merck Sharp & Dohme lsot. 

612-1209 Richmond St. 

London,Ont,Canada NGA 3L7 

Hans Grahm 


305 Bowne Hatt 


George Gray 


611Hansen Way 

ParD Atto, CA 94303 

Janet M. Griffiths 

Univ of Catif-Berketey 

Oept of Chem Engineering 


Angeta M. Gronenborn 

Max Planck Institute 

8033 Martinsried BE1 

Munich, FRG 

Herbert Gutowski 

Univ of Ittinois 


Urbana, IL 61801

Herbert Gutowski 



Champaign, 


Andreas Hackman 

Univ of Dortmund 

Inst. of Physics 

PO Box 500 500 

Dortmund,50, FRG D-4600 

Elizabeth Hajdu 

G. D. Searte & Co. 

4901Searte Parkway 

Skokie, IL 60077 

Gordon K. Hamer 

Xerox Research Center 

of Canada 

2660 Speakman Drive 

Nississuaga/Ont/Can LSK2L1 

willis B. Hammond 

ALlied Signal, Inc. 

PO Box 1021R 

Morristown, NJ 07960 

Ronatd L. Barter 

Univ. Catif 

Dept of Chem 

Santa Cruz, CA 9506/, 

V. Hariharasubramanian 

Univ of Pennsylvania 

Dept of Biochem & Biophys 

School of Medicine 


Cynthia J. Hartzelt 


Dept of Chemistry BG-IO 


John R. Havens 

Raychem Corp. 

300 Constitution Dr. 


Jane E. Hawks 

Kings College (KQC) 


Univ. of London 

Strnd/Lndn/Eng, UK WC2R 2L 

C.A.G. Haasnoot 

Unitever Research Lab 

Oliver van Moorttaan 120 

3133 AT Vlaardingen, 

Nedertand 

Grant W. Haddix 

Univ of Catif - Berkeley 

Dept of Chem Eng 


Laurance David Halt 

Cambridge Univ/MCCS 

Addenbrookes Hosp. 

Hilts Rd. 

Cambridge, UK 

Bruce E. Hammer 

Intermagnetics Gen.Corp. 

Hag. Resonance Res. Lab. 

1223 Peoples Ave. 

Troy, NY 12180 

Oc Hee Han 

Univ of Illinois 



Urbana, 1L 61801 

James A. Happe 

Lawrence Livermore 

National Lab 

PO Box 808 

Livermore, CA 94550 

Arnold M. Harrison 

Union Carbide 

PO Box 8361 

So. Charleston, WV 25303 

Dennis L. Hasha 

Oow Chemical Co. 

Analytical Labs Bldg 574 

Midland, MI 48667 

James F. Haw 

Texas A&M Univ 

ChemDept 


Geoffrey E. Hawks 

Queen Mary College-London 

Univ of London,Chem Dept. 

Mite End Road 

London,England, UK E14NS 

Fred Haberle 

Brucker Instruments 

Manning Park 


Edward W. Hagaman 

Oak Ridge National Lab 

Oak Ridge, TN 37831 

Ktaas Hattenga 

Michigan State Univ. 


East Lansing, M! 48824 

Terry E. Hammond 

Standard Oil of Ohio 

4440 Warrensvitte Rd. 

Cleveland, OH 44128 

Diane K. Hancock 

Nat'l Bur. of Stds. 

Btdg 222 A-361 


Gerard S. Harbison 

S.U.N.Y. Stonybrook 


Stony Brook, NY 11794 

J. Stephen Hartman 

Brock Univ. Chem. Dept. 

St.Catharines/Ont. L2S3A1 

Jon B. Hauksson 

Univ of Calif. Davis 

Dept of Chem 


Bruce L. Hawkins 

Colorado State Univ. 



Shigenobu Hayashi 

Univ of Illinois 

School Of Chem Science 

505 S. Mathews Ave. 

Urbana, IL 61801

Richard A. Hearman 

ICI PLC, C&P Group 

PO Box 90 

Middtesbrough, 

Cleveland TS6 8JE, UK 

Rose Anne HeLms 


600 Clemson Rd. 


P. Mark Henrichs 

Eastman Kodak Co. 

Research Labs 


Roy Hickman 




Howard Hill 


611Hansen Way 

ParD Alto, CA 94303 

Tetsu Hinomoto 

JEOL USA, INC. 


Peabody, MA 01960 

Yukio Hiyama 

NIH 

Btdg 30, Rm 106 


Tadeusz A. Hotak 




Xiaole Hong 



University Plaza 


Joseph P. Hornak 

Rochester Inst. of Tech. 



Nick J. Heaton 

Univ. of Calif.-San Diego 


Janet M. Henderson 


Hanover Ave. 

F[orham Park, NJ 

Hoby P. Hetherington 


Dept of Mot. Biophys 

and Biochem. 


Robert Highet 

Nat'[ Heart/Lung & Blood I 

National Inst. of Health 

Bldg 10 Rm 7N320 


David F. Hiltenbrand 

JEOL USA INC. 



Toshifumi Hiraoki 

University of Calgary 

Div. of Biochemistry 

Calgary,A[ta,Can. T2N1N4 

Gina L. Hoatson 

College of William & Mary 

Dept of Physics 

Williamsburg, VA 23185 

Scott K. Holland 


Sch of Med, Diag. Rad. 

333 Cedar St 


Robert S. Honkonen 


Eastern Research Ctr. 

Dobbs Ferry, NY 10522 

Howard Homing 


505 Julie Rivers Rd 


Gregory Helms 

Univ of Hawaii 

Dept of Chem - Manda 

2945 The MaLt 

Honolulu, HI 96822 

Michael J. Hennessy 

IGC Intermag. Gen. Corp. 

Magnetic Res. Lab. 

1223 Peoples Ave. 


J. Michael Hewitt 


Research Laboratories 


Lauren E. Hilt 


Oept of Chemistry 

East Lansing, MI 48824 

Peter R. Hitliard 

Ctairot Res. Labs. 

2 Blachtey Rd. 

Stamford, CT 06922 

Robert C. Hirst 

Goodyear Tire & Rubber 

Dept. 415A 

Akron, OH 44305 

Jeffrey Hoch 

Rowland Institute 

100 Cambridge Pkwy. 


Brenda S. Hotmes 

Naval Research Lab, 

Code 6120 


Kenneth D. Hope 

Univ of Atabama-Birmgham. 


University Station 

Birmingham, AL 35294 

David I. Houtt 

NIH 

9000 Rockvilte Pike 

Bethesda, MD 20892

Edward S. Hsi 

Union Carbide Corp. 

PO Box 670 

Bound Brook, gJ 08805 

Dee-Hua Huang 

University of Atabama 

NMR Facitity/CHS B-31 


Robert L. Hubbard 

Tektronix Inc. 

Box 500,MS50-324 

Beaverton, OR 97077 

Steven Huhn 

Nabisco Brands Res. Ctr. 

100 DeForest Ave. 

East Hanover, NJ 07936 

Catherine T. Hunt 

Rohm & Haas Co. 

Anatyticat Res 8B 

Spring House, PA 19477 

Stuart Hurtbert 

Burroughs Wellcome 

3030 Cornwattis Rd. 

Res Tri.Park, NC 27709 

Tracey Hutchins 

Chemicat Dynamics 

3001Hadtey Road 

PO Box 395 

So. Ptainfietd, NJ 07080 

David A. Ikenberry 

Univ of Catif.-San Diego 


B-014 


Dan Iverson 


611Hansen Way 

ParD Atto, CA 94303-0883 

Victoria J. Jacob 

Spectrat Data Services 

818 Pioneer 

Champaign, IL 61820 

Grace Hsu 

M & T Chemicats 

PO Box 1104 


Wen-Chang W. Huang 



Seattte, WA 98105 

Donatd W. Hughes 

McMaster University 


1280 Main St., West 

Hamitton,Ont.Canada L8S 4M 

Chi Cheng Hung 


Box 1134 



Brian K. Hunter 

Oueen's University 

Kingston, 

Ontario, Canada K7L 3N6 

Cynthia Husted 

Univ of [ttinois 

Box 43 Roger Adams Lab 

Sch. of Chem. Science 


WittiamC. Hutton 

Monsanto Co. 

Life Sci. NMR Ctr. 

700 Chesterftd. Vit.Pkwy. 


Paut T. Ingtefietd 

Ctark University 


Worcester, MA 01610 

Pradeep S. lyer 

Unocat 

Science & Tech.Div 

376 S. Vatencia Ave. 

Brea, CA 92621 

Russett E. Jacobs 

Univ. of Catifornia 

Dept. of Phys. & Biophys. 

Irvine, CA 92717 

Victor L. Hsu 

Univ. of Catif.-San Diego 

B-014 Dept of Chemistry 

La Jo[ta, CA 92093 

Shaw-Guand Huang 

Harvard University 


Cambridge, MA 02138 

David Hughes 


611Hansen Way 

ParD Afro, CA 94303 

David T. Hung 

Resonex 

720 Pa[omar Ave. 

Sunnyva[e, CA 94086 

Ratph E. Hurd 

GE NNR Inst. 



Howard Hutchins 

JEOL USA INC. 



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VPI & SU 



Ruth R. Inners 


Manning Park 

Vitterica, MA 01821 

Jasper Jackson 

120 Sherwood 

Los Atamos, NM 87544 

Nazim J. Jaffer 

Univ of Catifornia - L.A. 

Dept of Chem& Biochem. 

Los Angetes, CA 90024

Hans J. Jakobsen 

Univ of Aarhus 


800 Aarhus C, 

Denmark 

Erica Jansson 

Univ of Catif.-San Fran. 

Science 926 

Dept of Pharm. Chem. 


Ronald M. Jarret 

Cortege of Hoty Cross 

Dept of Chem. 

Worcester, NA 01610 

Lynn W. Jetinski 

AT&T Bert Laboratories 


Murry Hilt, NJ 07974 

LeRoy F. Johnson 

GE HMR 



Kermit M. Johnson 



East Lansing, Ml 48824 

Eric R. Johnston 

IBM Instruments, Inc. 

San Jose, CA 95110 

Robert L. Jones 

Georgia Tech 


Attanta, GA 30332 

Deborah A. Kattick 

UCAL, Berketey 

Lab for Chem. Biodynamics 

Catvin Lab, Dept of Chem 


Samue[ Kaptan 

Xerox Corp. 

800 Phittips Rd. 

0114 24D 

Webster, NY 14580 

Thomas L. James 

Univ of Catifornia 

PO Box 0446 


Norma Jardetzky 


Stanford Magnetic Lab 


Thomas P. Jarvie 




Yi Jin Jiang 


Deportment of Chemistry 

Box 102 

Satt Lake City, UT 8/,112 

Bruce A. Johnson 

Yate Univ./Sch of Med. 

Dept of Mot Biophys 

PO 3333 


Connie Johnson 


Manning Park 

git[erica, MA 01821 

Atan A. Jones 

Ctark University 


Worcester, NA 01610 

Tom Jue 

Yate University 

Mot Biophys & Biochem. 


Pau[ Kanyha 

GE NMR Institute 



Leeta Kar 

Univ. of Ittinois 

Dept of Ned. Chem 

PO Box 6998 


Nathan J. Janes 

Johns Hopkins Univ NIAAA 

1800 E. Jefferson St. 

Battimore, MD 21205 

Harotd C. Jarrett 

Nat't. Res. Councit-Canada 

Div. of Biotogica[ Science 

Ottawa,Ont. Canada K1A OR6 

Linda A. Jeticks 

Hunter cortege 

695 Park Ave. 

New York City, NY 10021 

Constantino Job 

Auburn lnternational-iMR 

4473 Wittow Rd. Ste. 105 

Hacienda Business Pk. 

Pteasonton, CA 94566 

James H. Johnson 

Hoffmann-La Roche 

340 Kingstand St. 

Btdg 71 

Nuttey,, NJ 07110 

Chartes S. Johnson, Jr. 

Univ of North Carolina 

Dept of Chem., 045A 

Chape[ Hitt, NC 27514 

Ctaude R. Jones 



W. Lafayette, IN 47907 

Gary P. Juneau 

Otin Corporation 

PO Box 586 

Cheshire, CT 06410-0586 

Lung Fa (Jeff) Kao 

Ctorox Tech Center 

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Pteasanton, CA 94566 

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Univ. of Catif.-San Fran. 

415 Warren Dr. #11 

San Francisco, CA 94131

Rodney V. Kastrup 

Exxon Research & Engineeri 

Rte. 22 E. CLinton Townshi 

Annandate, NJ 08801 

Lewis E. Kay 



225 Prospect St. 

Hew Haven, CT 06511 

James H. Keetar 

Cambridge University 

University Chemistry Lab 

Lensfield Rd. 

Canbridge, England CB21EW 

Tony Keller 


Manning Park 

Billerica, HA 01821 

Max A. Keniry 




Robert A. Kinsey 

BF Goodrich 

Res & Oeve[. Ctr. 

9921Brecksvitte Rd. 

Brecksvitte, OH 44141 

Branimir Ktaic 

Stanford Nag. Res. Lab 



Christopher T. G. Knight 

Univ. of Illinois 

Sch. Chemical Science 



Richard A. Komoroski 

Univ. of Ark for Hed.Sci. 

Slot 596 4301W. Markham 

Little Rock, AR 72205-71~ 

Alan M. Kook 

Rice University,NHR Ctr. 

Dept of Chemistry/Rm 309A 


Robert J. Kauten 

Univ. of California-Davis 

717 Atvarado #168 


David R. Kearns 


Dept of ChemB-014 


Paul A. Keifer 


School of Chem. Science 

Box 95-9 


Michael F. Ketty 

GE NMR Institute 


Fre~nont, CA 94539 

Gordon J. Kenned,/ 

Esso Petroleum Canada 

PO Box 3022 Research Dept 

Sarnia/Ont. Can. N7T 7141 

Agustin B. Kintanar 

University of Washington 

Dept of Chemistry/BG-lO 


Melvin P. Klein 

Univ. of Calif.-Berkeley 

Lawrence Berkety Lab 


Mark J. Knudsen 

Univ of California-Davis 

Dept of Biol. Chem. 

School of Medicine 

Davis, CA 95616-2043 

Hobby Kondo 

JEOL USA INC 



Max Kopetevich 

UCLA 


405 Hilgard Ave. 


Roger A. Kautz 

Stanford Medical Ctr. 

Dept of Cell Biotogy,DlO5 

Stanford, CA 94305 

Joseph D. Keegan 

GE NHR Institute 



Paul J. Keller 

Barrow Neurot. Inst. 

350 W. Thomas Rd. 

Phoenix, AZ 85013 

Raymond D. Kendrick 

IBM Research 

650 Harry Rd. 

San Jose, CA 95120-6099 

Albrecht Khuen 

Technical Univ of Berlin 

lwan-N.-Stanski-Inst. 

Str. 17 Juni 112,D-1000 

Berlin 12,Gerrnany 

Gregory L. Kirk 

Resonex 

720 Patomar Ave. 

Sunnyvale, CA 94086 

Jack Ktinowski 

Univ. of Cambridge 

Dept of Physical Chemistry 

Lensfietd Rd. 

CatTibrdg, Eng. CB21EP 

Frank E. Koehn 

Sea Pharm/Harbor Branch 

Oceanographic Inst. 

5600 Old Dixie Hwy. 

Ft. Pierce, FL 33450 

Marvin J. Kontney 

Univ. of Wisconsin 


1101 University Ave. 

Madison, gi 5]706 

Christoph Koppen 

Univ Bremn - FRG 

Physics Dept. 

2800 Bremen 33/FRG

Donald W. Kormos 

Case Western Univ. 


University Circle 


David Kramer 


533 Cabot Rd. 


V. V. Krishnamurthy 


Pest. Chem. & Tox. Lab. 


Atsushi Kubo 

Univ. British Cotu~ia 


2036 Main Matt 

Vancouver/Be,Can. V6T 1Y6 

Katsuhiko Kushida 


611Hansen Way 

Pa[o Alto, CA 94303 

Douglas N. Lamb 





David Lankin 


205 W. Touny Ave. 

Park Ridge, ]L 60068 

Dirk Laukiem 


Manning Park 


Ted Lawry 

Vet. Admin. Ned. Ctr. 

HRS Lab (11D) 

4150 Clement St. 


Joseph H.C. Lee 

Southern Illinois Univ. 

Dept of Chem. & Biochem. 

Carbondate, IL 62901 

Christine A. Kostek 

IBN Instruments 

Orchard Park 

PO Box 3332 


Thomas P. Krick 

Univ. Ninnesota 

Dept of Biochemistry 

1479 Gortner Ave. 

St. Paul, MN 55108 

Bata S. Krishnan 

Bristol Nyers Co. 

5 Research Pkwy. 

Wattingford, CT 06492 

Philip L. Kuhns 

Chemagnetics, inc. 

208 Commerce Drive 


Gittes Labette 

Cambridge Isotope Labs 



Joseph B. Lambert 

Northwestern Univ. 


Evanston, IL 60201 

Laurine A. LaPtanche 

Northern Illinois Univ. 


DeKatb, IL 60115 

Frank Laukiem 


Hanning Park 


W. John Layton 

Univ of Kentucky 

NRC 


Lexington, KY 40506-0053 

Robert W. K. Lee 



Riverside, CA 92521 

John F. Koztouski 


Dept. of Nedicina[ Chem. 


West Lafayette, lN 47907 

N. Rama Krishna 

Univ of Alabama 

NHR Core Fac. CHS B-31 


Richard W. Kriwacki 

Boehringer Ingelheim 

Pharmaceutical, Inc. 

90 E. Ridge Rd. 

Ridgefietd, CT 06877 

Ahi[ Kumar 


305 Bowne Hall 


Gerd N. LaMar 

Univ. of Calif.-Davis 


Andrew N. Lane 

NlHR-London 

The Ridgeway Nitl Hilt 

London, England NW7 1AA 

Ernest Douglas Laue 

Univ. of Cambridge 


Tennis Ct. Road 

Cambridge,England CB2 1QW 

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University of lttinois 

Biemedicat NR Lab 

1307 West Park 


Chang J. Lee 



Berkely, CA 94720 

Yu-Hwei Lee 

Univ. Illinois-Chicago 

Ned ChemDept 

833 S. Wo(xJ St. 

Chicago, II 60612

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Sun Refining/Hkting Co. 

PO Box 1135 

Narcus Hook, PA 19061-0835 

Hark Leifer 


611Hansen gay 


Hary Frances LeopoLd 




Nartin E. Levenson 

Auburn Int'[ IHR Div. 

Eight ELectronics Ave. 

Danvers Industrial Pk 

Danvers, HA 01923 

George C. Levy 

Neu Methods Research Inc. 


305 Bowne Hall 


Robert L. Lichter 

S.U.N.Y.Stony Brook 

2401 Lab Office BLdg. 

Stonybrook, NY 11794-4433 

Fu-Tyan Lin 

Univ of Pittsburgh 

1305 CB/ChemDept 


Peter Ltewettyn 


611Hansen Way 

Pa[o ALto, CA 94303 

George H. Lohrer 

Programmed Test Sources 

9 Beaver Brook Rd. 

Littteton, HA 01460 

Irving J. Lowe 

Carnegie MeLlon Univ. 

BiD[ Sci 



Suzannie C. Lee 

Proctor & GambLe Co. 

Miami VaLLey Labs. 

Box 39175 


PhiLip Leighton 

Univ of PennsyLvania 


Phita., PA 19104-6323 

CharLes L. Lerman 

ICI Americas 

Concord Pike & Hurphy Rd. 

gitmington, DE 19897 

John R. Levin 

General ELectric Co. 

199 Pomeroy Rd. 

Suite 104 

Parsippany, NJ 07054 

Barbara A. Lewis 

Univ. Wisconsin-Madison 


1101 University Ave. 


John J. Likos 

Honsanto Co. 

700 ChesterfieLd ViLLage P 


Shang-Bin Liu 

Univ. of CaLifornia 


HiLdebrand D-64 


H. Lock 

See abstract 

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Univ CaLifornia 

Div of Nature Sciences 

Santa Cruz, CA 95064 

Peter Luksch 

Scientific Info Services 

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Thomas Jefferson Univ. 

5 Jacatyn Dr. 

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Honsanto 018 

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Laura Lerner 

LCP/NIADDK/NIH 

Btdg 2 Rm B2-08 


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NIT 

NW14-5122 


Shi-Jiang Li 

Johns Hopkins 

Sch. Ned.310 TayLor 

720 RutLand Ave. 

BaLtimore, MD 21205 

Hans H. Limback 

Univ of Frieburg 

Physical Chemistry 

ALbert Str.21 

07800 Freiburg W.Ger 

David Live 

Emory University 


AtLanta, GA 30322 

Michael P. Lohrer 

Programmed Test Sourses 

9 Beaver Brook Rd. 

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Kingston Tech Inc. 

2235B Route 130 

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gestern Req. Res. Ctr. 


ALbany, CA 94710

P. R. Luyten 



La Jolta, CA 92093 

James W. Rack 

Nat't Inst. of Dent. Res. 

NIH Btdg 30 Rm 106 


Prem P. Mahendroo 

Atcon Laboratories, inc. 

6201S. Freeway 

Ft. Worth, TX 76134 

Paul D. Majors 

Lovetace Medical Found. 

2425 Ridgeorest Dr, SE 

Albuquerque, NM 87108 

Douglas R. Manatt 

Lawrence Livermore Lab 

Nuclear Chem, LLNL 

PO Box 808 L-233 


Steven R. Maple 

Indiana University 


Btoemington, IN 47405 

Charlene Marie 

Ctorox Tech Center 

7200 Johnson Dr. 


Trevor G. Marshall 

E.F. Unicon Systems Inc. 

3423 Hilt Canyon Ave. 

Thousand Oaks, CA 91360 

Gerald B Matson 

VA Nedica[ Center 

MRS Lab (11D) 



Nark Mattingty 


Manning Park 


James R. Lyerla 

IBM Almaden Res. Ctr. 

650 Harry Rd. 


Alexander G. Hacur 

Neu Methods Research inc. 



Vera V. Hainz 


Sch. of Chemical Sciences 

Box 34-1 

Urbana, 1L 61801 

J. Anthony Hatikayit 


Dept. HBB 

333 Cedar St. 

Neu Haven, CT'06510 

Sadasivam Manogaran 




Paul S. Marchetti 

Univ. of So. Carolina 


Cotun~ia, SC 29205 

Ron Raron 

Merck Institute 

Merck & Co., Inc. 

PO Box 2000 


Joel F. Martin 

Univ. Calif.-San Diego 

Dept of Radiology/H-756 


Shigeru Matsui 

Hitachi Central Res. Lab. 

Hitachi, Ltd. 

PO Box 2 

Kokubunji, Tokyo 185 Japan 

Anabeta Haynard 

Univ. of Toronto 

80 St. George St. 

Toronto, M55 1A1 Canada 

Gary E. Maciel 




Michael L. Haddox 

Syntex Corp. Res. Div. 

3401Hittview Ave. 

PaiD Alto, CA 94304 

Truett Majors 


611Hansen Way 

Pard At[o, CA 94303 

Stanley L. Manatt 

Jet Propulsion Laboratory 

4800 Oak Grove Dr. 


Jintong MaD 

University of Florida 

HRI Group 



Thomas H. Hareci 

University of Florida 

Radiology Dept 

Box J-374 


Brian J. Marsden 

Univ. of Alberta 

Dept of Biochem. 

Edmonton, 

Alberta, Canada T6G 2H7 

G. D. Mateescu 

Case Western Resrv. Univ. 


George Hattinger 


533 Cabot R. 


Charles L. Nayne 



Salt Lake City, UT 84112

John HcAutiffe 

Univ of Cincinnati 

Oept of Anesthesia 

231Bethesda Ave. 


Lewis NcDonald 

JEOL USA INC. 



Stuart J. McLachlan 

General Electric Co. 



Lee McPeters 


PO Box 219 

Bristol, PA 19007 

Ronatd A. Merrill 

YaLe University 

Sterling Chem Lab 

PO Box 6666 

New Haven, CT 06511-8118 

Frank Michaets 

Eastman Kodak Res. Labs. 

Eastern Ave. 


PameLa A. Mitts 

Univ of Calif.-San Fran. 




AT&T BeLt Labs 


Murray HILL, NJ 07974 

ore Mots 

gayne State Univ. 


Detroit, Ml 48202 

Courtney F. Morgan 

Univ. of CaLif.-Santa Cruz 

Natural Sciences It 


Mark A. McCoy 

Frick Chemical Lab 

Washington Road 


Jacquetine L. McGourty 

Univ. of CaLif.-Davis 



fan J. McLettan 

Johns Hopkins Ned. Sch. 


BaLtimore, MD 21205 

James H. Medley 

BristoL-Myers 

Pharm. Res. & Dev. Div. 

PO Box 4755 

Syracuse, NY 13221-4755 

Kenneth R. Metz 

Penn State Univ. 

Hershey Red. Ctr/Rad.Dept. 

PO Box 850 


John M. Mittar 



PO Box 6666 


Michael J. Minch 

Univ. of Pacific 

Dept of Chem. 

Stockton, CA 95211 

Hitoshi Miura 

E356/113,CR.D, 

E.].DuPont de Nemours 


Ben Montez 

818 Pioneer 

Champaign, IL 61820 

Paul K. Morris 

Morris Instruments Inc. 

1382 McMahon Ave. 

GLoucester, 

Ontario, Canada K1T 1C3 

Paula L. McDaniet 



Box 35-1Dept of Chem. 


Robert A. McKay 

gashington University 

Dept of Chem/Camp Bx1134 

1Brookings Dr. 


Ronatd McNamara 

Univ. of PennsyLvania 


PhiladeLphia, PA 19104 

Michael T. Melchior 

Exxon Research 

Clinton Township 

Annandate, NJ 08801 

Dieter Meyerhoff 




Joel B. HilLer 

Naval Research Lab 

Code 6120 


Virginia W. Miner 

Dow Chemical Co. 

Btdg 574 

Midland, MI 48667 

Steven C. Mohr 

GE NNR Instruments 



J. Robert Mooney 

Standard OiL Co. 

4440 Warrensvilte Ctr Rd. 


George O. Morton 


Lederte Labs Div. 

Pearl River, NY 10965

Michael E. Noseley 

Univ of California -S.F. 


Box 0446 


Donald D. Huccio 

Univ. Of ALabama 



Nartha P. Nurari 

Liposome Technology Inc. 

1050 Hamilton Court 


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Box 0446 


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Lockheed Hiss. & Space Co. 

0/48-92 B/195B 

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Sunnyvale, CA 94088-3504 

Lewis E. Nance 

Univ. of North Carolina 


601S. College Rd. 

Wilmington, NC 28403-3297 

Sarah J. Nelson 

Fox Chase Cancer Center 

NHR Labs 

77'01Burhotme Ave. 


David G. Nettesheim 

Abbott Labs 

D-47G, AP9 


Xuan-Zhong Ni 



Colun~oia, SC 29223 

Ann T. Nicot 

Litton-Guidance & Control 

5500 Canoga Ave. 

Woodland Hilts, CA 91365 

Edwin Hotelt 


San Francisco State Univ. 

1600 Holtoway Ave. 


Karl T. Muetter 

Univ of Calif.- Berkeley 



James B. Murdoch 

Picker Inter. 

NHR Division 

5500 Avion Park Dr. 

Highland Heights, OH 44143 

Martin S. Mutter 

McNeil Pharmaceuticats 

Dept of Chemical Research 

Sprg. House, PA 19477-0776 

Donald L. Naget 

Eppley Institute 

Univ. Nebraska Ned Ctr. 

Omaha, NE 68105 

Surinder Singh Naruta 

Scripps Clinic & Research 

Dept of Notecutar Biol. 

10666 g. Torrey Pines Rd. 


Janis T. Nelson 

Syntex Research 

3401Hittvieu Ave. 

Pa[o Alto, IL 60566 

Richard A. Ne~anark 

3N Co. 

Btdg 201-BS-05 

St. Paul, NN 55144 

Brenda C. Nichols 


533 Cabot Rd. 


Ronatd A. Nieman 

Arizona State University 


Tempe, AZ 85287 

Foad Mozayeni 

Akzo Chemie America 

8401W. 47th St. 

NcCook,, IL 60525 

Detteff Nuetter 


Nanning Park 

Bitterica, MA 01821 

Paul Murphy 

IBM Instruments Btdg 1 

Orchard Park 


Mark E. Myers 

General Motors Res. Lab. 

30500 Mound Road 

Warren, Ml 48090-9055 

Thomas T. Nakashima 

Univ of ALberta 


Edmonton, 

Atta.,Canada T6G 2G2 

Vitas garutis 

gatco Chemicals 

One Nalco Center 

gaparvitte, IL 60566 

Janis T. Nelson 

Syntex Research 

3401Hittvieu Ave. 

Paid Alto, CA 94304 

Richard D. Neumark 

Laurence Berkeley Lab 

MS 55-121 

1 Cyclotron Road 

Berkeley, CA 947"20 

Linda Nichotson 

Florida State University 

Inst. Hote.Biophys. 

Tallahassee, FL 32306 

Walter P. Nienczura 

University of Hawaii 


Honolulu, HI 96822

Robin A. Nissan 

Naval Weapons Center 

Code 3851Nichetson Lab 

China Lake, CA 93555 

Atsuko Y. Nosaka 

NIH 

Nat't Inst. of Aging 

Gerontology Center 


Coteen Young O'Gara 

Wayne State Univ. 


410 W. Warren Ave. 

Detroit, N! 48202 

Mark A. O'Neil-Johnson 


40 Airport Pkwy. 


Jong H. Ok 




ALan W. Otson 

General Electric NHR 

3165 Ludlow Rd. 

Shaker Hgts., OH 44120-283 

Anita M. Orendt 

Univ of Utah 

Chemistry Dept/Box 6G 


James D. Otvos 


at Nitwaukee 


Nitwaukee, W! 53201 

Peter J. Paterson 

JEOL USA INC 

11 Dearborn Rd 


Ross Payne 


611Hansen Way 

Pato Alto, CA 94303-0883 

Joseph H. Noggte 

University of Delaware 



Rudi Nuntist 




John F. O'Gara 

General Ntrs Tech Res. Lab 

30500 Hound R. 

Warren, N! 48090-9055 

Terrance G. Oas 

NIT 

Francis Bitter Natl Nag. L 


Eric Otdfietd 


Sch. of Chemical Science 



Stanley J. Opetta 



PhiladeLphia, PA 19104 

Donald G. Ott 

Los Atamos Nat't. Lab. 

Exptos. Tech. Group 

MSG-920 

Los Atames, NN 87545 

Allen R. Palmer 

Chernagnetics 


Ft Collins, CO 80524 

Steven L. Patt 


611Hansen gay 


Robert N. Pearson 

3590 Churchitt Ct. 

Auburn Int~l IMR Div. 


Carol I. Noggte 

Medtab, Inc. 

8 Falcon Court 


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Chemagnetics, Inc. 


Ft. ColLins, CO 80524 

Daniel J. O'Leary 

UCLA 


Los Angeles, CA 

Nuneki Ohuchi 

JEOL Ltd. 

Nakagami Akishima 

Tokyo, Japan 196 

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Abbott Labs Btdg AP9 

Pharmaceutical Discovery 


Arnulf Oppett 

Siemens A. G. 

Henkestr 127 

D-8520 

Erlangen, FRG 

Albin Otter 

Univ of Alberta 


Edmonton, 

Alta, Canada TSG 2G2 

Jonathan W. Paschal 

Eli Lilly Res. Labs. 

Lilly Corp. Center 

Indianapolis, 1N 46285 

John Paxton 


611Hansen Way 

Palo Alto, CA 94303 

Gerald A. Pearson 

Univ of Iowa 


Iowa City, IA 52242

Joseph H. Pease 


Melvin Calin Lab 


Donald J. Pennino 

The B.O.C. Group Inc. 


Nurray Hill, NJ 07974 

Carote Perry 

Univ of Utah 



David H. Peyton 

Univ of Catif.-Davis 



Stephen B. Phitson 

Univ. of Minnesota 

Dept of Chem. 

207 Pleasant St., SE 

Minneapolis, MN 55455 

T. Phil Pitner 

Boehringer lngelheim 

90 E. Ridge/PO Box 368 

Ridgefie[d, CT 06877 

Mark D. Potiks 

Univ. of Connecticut 

Inst. of Materials Science 

U-136 

Storrs, CT 06268 

Ftemming M. Poutsen 

Cartsberg Labs 

Dept of Chem. 

Gamte Carlsberg VEJIO 

DK-2500 Vatby, Copenh Denma 

William Proctor 

Oxford Instruments 

3A Alfred Circle 

Bedford, HA 01730 

Jin Oiao 

San Diego State Univ. 



James J. Pekar 

Univ. Of Pennsylvania 

Dept of Biochem/Biophysics 


Ray Perkins 




Joseph J. Pesek 

San Jose State Univ. 



Minh Tan Phan Viet 

Univ. of Montreal 


PO Box 6128, Sta. A 

Montrt,Oue,Can. H3C 3J7 

Francis Picart 

Rockefeller Univ. 

Box 299 


New York, NY 10021 

Steven M. Pitzenberger 

Merck Sharp & Dohma Res. 

Btdg 26o100 

West Point, PA 19486 

Karl Heinz Pook 

Boehringer lngetheim KG 

Analytical Chem. 

6507 Ingetheim 

Rhein, West Germany 

Thomas K. Pratum 


Dept of Chemistry, BG-IO 


Ronatd J. Pugmire 

Univ. of Utah 

304 Park Btdg 


Michael J. Ouast 

UTMB-Galveston 

200 University Blvd. 

St. 601 


Jeffrey G. Petton 


Melvin Calvin Lab 


Thomas G. Perkins 

GE NMR, Instruments 



Hark A. Petrich 


Dept of Chem. Eng. 


Martin A. Phitlippi 

Chtorox Co. 

PO Box 493 

Pleasanton, CA 94566 

Ross G. Pitcher 

Hoffman LaRoche 

Physical Chemistry Dept. 

Nutley, NJ 07110 

Nick Ptavac 

Univ of Toronto 


80 St. George St. 

Toronto,Ont,Canada MSS 1A1 

Michael A. Porubcan 

E.R. Squibb 

PO Box 4000 


James H. Prestegard 




David E. Purdy 


186goodAve., So. 

Iselin, NJ 08830 

Gregory Ouinting 



Ft. Collins, CO 80523

Dattas L. Rabenstein 




Tom Raidy 




Margaret H. Rakowsky 

Naval Research Lab. 

Code 617] 

Washington, DC 20375 

Mark A. Rance 

Res. Inst. of Scripps Ctin 

10666 N. Torrey Pines Rd. 


Betty M. Rather 

Pennwatt Co. 

900 First St. 

King of Prussia, PA 19406 

John M. Read 

DuPont Medical Prod. Dept. 

E336/29 

gilmington, DE 19898 

Robert A. Reamer 

Merck Sharp & Dohme 

PO Box 2000, Btdg 801-210 


Christina Redfietd 

Univ. of Oxford 

Inorganic Chemistry Lab. 

South Parks Road 

Oxford, England, UK OXl 30 

william F. Reynolds 

Univ. of Toronto 


Toronto,Ont.,Canada M5S 1A 

Rene Richarz 


611Hansen Way 

ParD Alto, CA 94303 

Dan Raftery 

Univ. of Catif.-Berketey 

Hitderbrand D-60 


Ponni Rajagopat 

UCLA 


c/o Jutie Feigon 


Daniel P. Raleigh 

MIT/Rm NW 14-5107 

77Massachusetts Ave. 


Chris I. Ratctiffe 

Nat't. Res. Council Canada 

Ottawa, Ont, Can. K1A OR6 

Bruce David Ray 

IUPUI Physics Dept. 

PO Box 647 

Indianapetis, IN 46223 

David B. Reader 

Cambridge Isotope Labs 



Gade S. Reddy 

DuPont Central Research 

E328 


Jeffrey A. Refiner 

Univ of Calif.-Berkeley 

Dept Chem. Eng. 

201 Gilman Hall 


Anthony A. Ribeiro 

Duke University 

Box 3711 

Durham, NC 27710 

John Rieger 



Sugar Land, TX 7"/478 

John I. Ragte 

Univ. of Massachusetts 

Dept of Chemistry, 

LGRT411 

Amherst, HA 01003 

Srinivasan Rajan 

American Cyanamid 

PO Box 400 


John Ralph 

Univ of Calif.-Berkeley 


Berkety, CA 94720 

Alan Rath 


CNID, Cancer Ct. Rm 228 

Albuquerque, NM 

G. Joseph Ray 

Amoco Research Center 

PO Box 400 

Napervitte, IL 60566 

Lyn Ream 

Auburn Int't. IMR Oiv. 

4473 Willow Rd. 

Hacienda Business Park 

Pteasonton, CA 94566 

Richard D. Redfearn 

Marshall Res. & Dev. Lab. 

DuPont 

3500 Grays Ferry Ave. 


Linda G. Reven 



505 S. Mathews Rd. 


Metanie Rice-Bernatzki 


611Hansen Way 

Pa[o Alto, CA 94303 

Errott S. Riewerts 

Southwest Research lnst. 

PO Box 28510 

San Antonio, TX 7828/,

Peter Rinatdi 




WiLLiam H. Ritchey 




Valerie J. Robinson 

Syntex, inc. 

2100 Syntex Ct. 

Mississuaga, 

Ontario, Can. L5N 3X4 

JtxJy C. Rodeghero 

Clorox Tech Center 

Analytical Res. & Serv. 

7200 Johnson Dr. 

Pleasanton, CA 94566 

Stephen B. W. Roeder 

San Diego State Univ. 



WiLliam D. Rooney 

S.U.N.Y.-Stoneybrook 


Stoneybrook, NY 11794 

Kenneth 0. Rose 

Exxon Research & Engineeri 

CLLAB/LH170 

Annanda[e, NJ 08801 

Daniel W. Roth 

Amplifier Research 

160 School House Rd. 

Souderton, PA 18964-9990 

Steven P. Rucker 

Univ. of Calif.-BerkeLey 


Serketey, CA 94720 

Jacques Rutschmann 

Diasonics, inc. 

533 Cabot Rd. 


James H. Riordan 

Southern Research inst. 

PO Box 55305 

Birmingham, AL 35255-5305 

Christopher D. Rithner 

Warner Lan~bert 

2800 Plymouth Rd. 

Ann Arbor, M1 48105 

Thomas J. Robinson 

3H Co./Riker Labs 

3N Center/Bldg 270-4S-02 

St. PauL, HN 55144 

James C. Rodgers 


Oept of Chemistry, B-014 

La Jolla, CA 92093 

William L. Rottuitz 

Southwest Research Inst. 

6220 Cutebra Rd. 

PO Box 28510 

San Antonia, TX 78284 

Thatcher W. Root 


Dept of Chem. Eng. 

Hadison, WI 5]706 

Scott Ross 

Cattech, 12772 


T. Michael Rothgeb 

Proctor & Gamble 

lvorydale Tech. Ctr. 

5299 Spring Grove Ave. 


Randat Rue 


1120 Auburn Street 


Timothy R. Saarinen 

Univ. of North Carolina 


Chapel Hill, NC 27514 

John A. Ripmeester 

Nat't. Res. Council-Canada 

Div of Chemistry 

Ottaua,Ont.,Canada K1A OR9 

James E. Roberts 


Chem. Dept/Btdg.6 


Ronatd K. Rodebeugh 

CIBA-GEIGY Corp. 

444 Sa~nilt River Rd. 

Ardstey, NY 10502 

D. Christopher Roe 

OuPont Experimental Sta. 

Central Research E356 


Alan Ronemus 


Chem Dept B-014 


Richard C. Rosanske 

Florida State Univ. 


Tatlahassee, FL 32306-3006 

Klaus Roth 

V.A. Ned. Ctr-San Fran. 

NHR Lab (110) 



David J. Ruben 

National Hagnet Lab,HIT 

170 Albany St. 


John G. Russell 

California State Univ. 


Sacramento, CA 95819 

Paul Sagalyn 

Army Materiats Tech Lab. 

SLCNT-OMM 

Dept of the Army 

Watertown, HA 02172-0001

Ronald Sager 

Quantum Design 

11568 Sorento Valley Rd. 

Suite 15 


Robert E. Santini 


Chemistry Dept #92 

West Lafayette, IN 47907 

Indrani Sarkai 

Vittanova 

Viltanova, PA 19085 

James D. Satterlee 

Univ of New Mexico 


Albuquerque, NM 87131 

Brian Sayer 

McMaster University 


1280 Main St.,West 

Hmttn,Ont,Canada L8S 4M1 

Robert A. Schiksnis 


Dept of Chemistry D5 


Kirk Schmitt 

Mobile Res. & Dev. 

PO Box 1025 

Princeton, gJ 08540 

Everett C. Schreiber 

G.E. NMR 



Jay F. Schutz 

Henkel Research Corp. 

2330 Circadian Way 

Santa Rosa, CA 95407 

Emil M. Scoffone 




Felix Satinas, Ill 

Univ. Texas Med. Branch 

200 University Blvd. Ste 6 


Armando DeLos Santos 

Southwest Res. Inst. 

6220 Cutebra Rd. 

San Antonia, TX 78284 

Susanta K. Sarkar 

Smith Ktine & French 

L-940 PO Box 7929 


John K. Saunders 

Nat'l Res Council of Canad 

Div. of Biological Science 

Ottawa,Ont,Can. K1A OR6 

Terrence A. Scahitt 

Upjohn Co. 

Physical & Analytical Chem 


Thomas Schteich 




Charles Schramm 

Catalytica Assoc., Inc. 

430 Ferguson Dr. 

Mountain View, CA 94043 

Jane K. Schreiber 

G.E.NMR 



Herbert M. Schwartz 

Renssetaer Polytechnic Ins 



Katherine N. Scott 

Univ. Florida 

Miller Health Ctr. 



Everett R. Santee, Jr. 

Univ of Akron 

Institute Polymer Science 

302 E. Buchtel Ave. 


K. P. Sarathy 

Auburn University 


Auburn, AL 36849 

Shiro Satoh 


611 gansen Way 

ParD Atto, CA 94303 

Francoise Sauriot 

McGitt University 


Montreat,Oue,Can. H3A 2K6 

Jacob Schaefer 




Petra Schrnatbrock 

Ohio State University 

MRI Facility 

1630 Upham Drive 


Suzanne E. Schramm 

Mobile Res. & Dev. Ctr. 

PO Box 1025 

Princeton, RJ 08540 

Regina Schuck 

G.E. NMR Inst. 



Arnold L. Schwartz 




Kenneth L. Servis 

Univ of So. Calif. 


Los Angeles, CA 90089-1062

Naresh K. Sethi 

Univ. of Utah 


Bx132, Henry Eyrng.Btvd. 


Bernard L. Shapiro 

Texas A & M Univ. 



Peter Shepard 

John Wiley & Sons, Ltd. 

Baffins Lane 

Chichester, 

Sussex, England, UK 

Yang T. Shieh 



CLeveland, OH 44106 

Sakae Shiojima 

JEOL USA INC. 



Ben A. Shoulders 

University of Texas 


Austin, TX 78712 

Ronatd E. Siatkowski 

Naval Reserch Lab 

Chemistry Division 

Code 6122 


Connie S. Sitber 

gakefietd Corp. 

3131A East 29th St. 

Bryan, TX 77802 

Virgil Simptaceanu 

Biotog. Sci/Carnegie Metro 


Pittsburgh, PA 15213-2683 

Larry D. Sims 

Univ. of Houston 

4800 CaLhoun 


A. J. Shaka 




Michael J. Shapiro 

Sandoz Research Inst. 

NMR Facilities, Rte 10 

East Hanover, NJ 07936 

Donald R. Shepherd 

AmpLifier Research 

160 School House Rd. 

Souderton, PA 18964-9990 

Carl M. ShieLds 




Ata Shirazi 

Univ of CaLifornia 



Litian G. Shum 

Avery International 

325 N. Altadena Drive 


Hanna Siezputowski-Gracz 

Univ of Missouri 

Biology Dept. 

Columbia, NO 65211 

Robin F. Sitverman 

ClBA-Geigy Corp. 

556 Morris Ave. 


Etena Simptacenau 

Carnegie MeLton Univ. 

Ct. Biomed. Res. MeLLon In 


Pittsburgh, PA 15213-2683 

Dean g. Sindorf 

Chemagnetics 


Ft. Cottins, CO 80524 

Xi Shan 

Univ. Of IlLinois 

Box 4-1NL 



Robert L. Shetdon 


611Hansen Way 

Pato Alto, CA 94303 

Mark H. Sherwood 

Univ of Utah 



Nancy R. Shine 

ICR, Pacific Presb. 

Medical Center 

2200 Webster St. 


James N. Shoo[ery 


611Hansen gay 

Pa[o ALto, CA 94303 

Dikoma C. Shungu 

Hershey Medical Center 



Steve K. Silber 

Texas A & M University 


Cortege Station, TX 77843 

Diana R. Sirnonsen 


Sterling Chemical Lab 



Marjorie Simpson 

Univ of Calif. Berkeley 



David J. Single 

Harvard University 


12 Oxford St. #90 

Cambridge, MA 02138

Robert Skarjune 

3M Company 

Btdg 201-BS-OS/3M Ctr. 

St. Paul, MN 55144 

George Stomp 


Physical & Analytical Chem 

7255-209-006 


Karen Ann Smith 

Colgate-Palmolive Co. 

909 River Road 

Piscataway, NJ 08854 

Letand L. Smith 

Univ of Texas 

Medical Branch 


Steven O. Smith 

NW14-5107/M1T 

Nat't Rag Lab 

170 Atbeny St. 

cambridge, HA 02139 

Richard Snook 




Mark S. Solum 

Univ of Utah 


HEB #132 


Christopher H. Sotak 

GE NMR Instruments Inc. 



Charles S. Springer, Jr. 

State Univ of New York 


Stony Brook, NY 11794-3400 

Ruth S. Stamaszek 


North Chicago, IL 60064 

Tore Skjetne 

Sintef, Tronc~eim 

Center for NMR 

N-7034 Trondheim Noruay 

Catherine Stomp 

Medical Theraputics, 

9162-243-67 


Kalamazoo, Nl 49001 

Martin A. R. Smith 

Bruker Spectrospin-Canada 

555 Steetes Ave. E. 

Milton, Ont,Canada L9T 146 

Michael B. Smith 

Henry Ford Hospital 

NMR Facility Dept Neur. 

2799 W. Grand Blvd. 

Detroit, Ml 48202 

Wanda S. Smith 




Arlen Soderquist 



Salt Lake City, UT 8/,121 

ore Sorenson 

Eth Zurich 

Physical Chem Lab 

Eth Zentrum 

8092 Zurich Switzertnd 

Steven W. Sparks 

National Inst. Health 

Btdg 30/RmlO6/NIDR 


J. B. Sptizmesser 




John D. Stanley 

Heu Methods Research 

719 E. Genessee St. 

Syracuse, HY 13210 

Vtadimir Sklenar 

NIH, Lab Chem Phys, 

NIDDK, 2/Rm B2-22 


Steve H. Smattcembe 


611Hansen Way 


Rebecca L. Smith 


Analytical Research 

727 Norristown Rd. 

Spring House, PA 19477 

Stanford L. Smith 

Univ of Kentucky 

MR/SC 

101 Stone Bldg. 

Lexington, KY 40506-0053 

William B. Smith 

Texas Christian Univ. 


Fort Worth, TX 76129 

Nicholas Soffe 




Oxford, England, UK 

Steven D. Sorey 

University of Texas-Austin 


Austin, TX 78712 

Richard F. Sprecher 

DOE, PETC 

PO Box 10940 


Naurice St-Jacques 

Univ of Montreal 


Montreat,Ont,Can H3C3J7 

Piotr M. Starewicz 


186 Wood Ave., So. 

Isetin, NJ 08830

Ruth E. Stark 

College of Staten Island 

CUNY 

Staten Is,and, NY 10301 

Richard L. Stephens 


D418,AP9 

North Chicago, IL 60004 

Phoebe L. Stewart 



Phita., PA 19104-6323 

Gerald N. Stockton 


Agricultural Res. Div. 


David Stranz 

E.I.Dt~Pont Agr. Prod. Dept 

Experimental Station 


Nark J. Sullivan 

Hercules, inc. 

Research Ctr. 


Dieter Suter 




Fred J. Swiecinski 

USl Chemicals, Inc. 

3100 Golf Rd. 

Rolling Neadows, IL 60008 

Nikotaus Szeverenyi 

S.U.N.Y. Health Science 


708 Irving Ave. 


Christian I. Tanzer 


Nanning Park 


Jonathan F. Stebbins 


Dept of Geology 


Larry L. Sterna 

Shell Development Co. 

PO Box 1380 


Robert C. Stewart 

~unoco Prod. Research 

4502 E 41st St. 

PO Box 3385 

Tulsa, OK 74102 

Gerhard Stoeckt 

Scientific Info Services 

7 NoodlandAve. 

Larchmont, NY 10538 

Jane Strouse 




GLenn R. Sullivan 

GE NNR Instruments Inc. 



Jerome D. Swalen 

IBM 

Almaden Res. Ctr. 

K-34/802, 650 Harry Rd. 


Brian D. Sykes 

Univ of ALberta 

Oept of Biochemistry 

Edmonton, 

ALberta, Canada T6G 2H7 

Kiyonori Takegoshi 




Herbert Taus 

GE NNR Instruments, Inc. 



Edward O. Stejskat 

North Carolina State 


Box 8204 

Raleigh, NC 27695-8204 

Edward Sternin 

Univ of British Columbia 


Vancvr.BC,Canada V6T2A6 

Peter Stitbes 

Royal Inst Tech 

S-10044 Stockholm, Sweden 

Waldehar Stoecktern 

IBH 

650 Harry Rd. 

San Jose, CA 95120-6099 

Biing-Ning Su 

Stauffer Chemical 

Eastern Res. Ctr. 

Dobbs Ferry, NY 10522 

Richard H. Sullivan 

Jackson State University 

PO Box 17636 

Jackson, MS 39217 

Linda Sweeting 

Towson State University 


Baltimore, HD 21204 

Linda L. Szafraniec 

Chem Res. Dev. & Eng Ctr. 

SNCCR-RSC-P 

Abrdn Prv Grnd., MD 21010- 

Jau Tang 

Argonne National Lab 

Chemistry Division 


Robert E. Taylor 


Nanning Park 

Bitterica, NA 01821

R. Tearson 

See program 

Ann N. Thayer 

AT&T BeLt Labs 


Murray HiLt, NJ 07974 

Arthur R. Thompson 

Argonne Nat'l Lab 

Chemistry E169 

9700 S. Cass Ave. 


Victor Tong 

TecNag 

6006 Bettaire BLvd. 


Beau James Toy 

Univ of Catif- San Fran. 

401 Gold Street 

Auburn, CA 95603 

James Tropp 


533 Cabot Rd. 


Rayond Tse 

Desoto Inc. ACAR 

1700 S. Mt Prospect Rd. 

Des Ptaines, IL 60017 

Gary L. Turner 

SpectraL Data Services 

818 Pioneer 

Chanpaign, IL 61820 

Feng-Fang Tzeng 

Univ. of Catif-Riverside 



Stephen ULrich 




Mike Tesic 


611Hansen Way 


WiLLiam J. Thoma 

Fox Chase Cancer Ctr. 

NMR lab 

7701 Burhotme Ave. 

Phitadetphia, PA 19111 

Robert L. Thrift 


255 fourier Ave. 


Dennis A. Torchia 

Nat'[ Inst. of HeaLth 

Btdg 30, Rm 106 


Daniel O. Traficante 

Univ of Rhode Island 


Kingston, R! 02881 

Pearl Tsang 

Scripps CLinic & Res. Foun 

10666 Toney Pines Rd. 


Chien Ken Tseng 


1200 S. 67th St. 


Anne H. Turner 

Howard University 


Washington, DC 20059 

Nathan Tzodikov 

G.E. NMR Instruments Inc. 



Sun Un 


Chem. Biodynamics Lab LBL 


Venkataraman Thanabat 

Univ of Calif.-Davis 



Hans Thomann 

Exxon Corporation 

Exxon Cord. Res. Lab 

AnnandaIe, NJ 0~01 

Hye Kyung C. Timken 



505 S. Matheus Ave. 


David R. Torgeson 

Mid-Continent Instruments 

2327 N. Dakota Ave. 

Ames, IA 50010 

Lynda G. Treat-Ctemons 


SMRL 


Rotf Tschudin 

Nat'L. Inst. of Health 

Btdg 2, RmB2-02 


David Turner 

Pennzoit Tech. Ctr. 

PO Box 7569 

The Woodlands,, TX 77387 

Christopher J. Turner 

Columbia University 

Box 555 Havermeyer Halt 


Kamit Ugurbit 

Univ of Minnesota 

GFWBI 

Navarre, MN 55392 

Steve W. Unger 

Univ of CaLif.-Davis 

NMR FaciLity MS-1A 

Davis, CA 95616

Timothy Vail 

Chem Dynamics Corp. 

PO Box 395 

3001 Hadley Rd. 

S. PLainfield, NJ 07080 

Joseph B. Vaughn 

Rockefeller University 



Alexander J. Vega 

DuPont Experimental Sta. 

E356 


Ronatd E. Viola 

Univ of Akron 



Tom Walter 


Box 22 Noyes Lab 


Jin-shan Wang 

Virginia Potytech. & SU 

Dept of Vet. Biosciences 

College of Vet Med. 


Raymond L. Ward 

Lawrence Livermore Labs 

Box 808, L-310 


Andrew L. Waterhouse 

Tutane University 


New Orleans, LA 70118 

Gretchen G. Webb 


Dept of Chem 



David Weisteder 

US Dept of Agriculture 

Northern Regionat Res. Ctr 

Peoria, IL 61604 

Kathteen G. Valentine 


ChemDept. Frick Lab 


David M. Vea 


505 Jutie Rivers Road 


Vincent S. Venturetta 

Anaquest/BOC Tech Ctr. 


Murray Hilt, NJ 07974 

Chartes G. Wade 


40 Airport Pkuy 


Chuan Wang 

Rutgers College 


Piscataway, NJ 0~54 

Pu Sen Wang 

Monsanto Research Corp. 

Mound Ave. 

Miamisburg, OH 45342 



Frick Chemical Lab 



Charles L. Watkins 

Univ. of ALabama 



Jon O. Web[) 

M-R Resourses Inc. 

PO Box 642 


Ashburnham, HA 01430 

Daniet P. Weitekamp 

CatTech 

Noyes Lab of Chem. Phys. 


David VanderHart 

Nat'[ Bureau of Stds. 


W. S. Veeman 

See program 

Daniel g. Vigneron 

Univ of Calif.-San Fran. 



Frances Ann Walker 

San Francisco State Univ. 



Hsin Wang 

Eastman Kodak Res. Lab 

B[dg 82/FL1 


Mark A. Ward 

Natco Chemical Co. 

PO Box 87 


Dennis L. Warrenfe[tz 

Univ. of Georgia 

CCRC Russet[ Labs 

Athens, GA 30613 

John S. Waugh 

Mass Inst. of Tech. 

6-235 



Jarma P. Wehrte 

Johns Hopkins Univ. 

Sch of Med/Dept Rad. 


Larry B. We[sh 

ALlied Signal EMRC 

50 East Atgonquin Rd. 

Des Ptaines, IL 60017

David E. Wemmer 




Nito Westter 

Univ. of Wisconsin 


420 Henry Natl 


David R. Wheeler 

Cattech 164-30 


David J. Wilbur 


611Hansen Way 


Philip G. Williams 

Nat't. Tritium Labeling 

Lawrence Berkeley Lab 

UCALLBerketey 


Kenneth L. Wittiamson 

Nount Holyoke College 


South Hadley, MA 01075 

Donald M. Wilson 

Chevron Research 

576 Standard Ave. 


Robert A. Wind 




Scott E. Woehter 



University Plaza 


Gerd Wolff 


Manning Park 

Bilterica, NA 01821 

Laurence G. Werbetou 

Hew Mexico Inst. of 

Nining Technotogy 


Socorro, gN 87801 

Stephen N. Wharry 

Phillips Petroleum 

144 P.L. 

Barttesvitte, OK 74004 

Earl B. Whipple 

Pfizer Inc. 

Central Research Labs 

Groton, CT 06340 

M. Robert Willcott 

NHR Imaging, Inc. 

2501-C Central Pkt~/ 


Wanda F. Wittiarns 

Allergen Pharmaceuticals 

Dept of Anaty. & Biopharm. 

2525 DuPont Dr. 

irvine, CA 92713 

Daniel Wittiamson 

Epptey Institute 

Univ. of Nebraska Red. Ctr 

Omaha, NE 68105 

G. Edwin Wilson, Jr. 

Univ. of Akron 



Toni Wirthlin 


611Hansen Way 

Palo Alto, CA 94303 

Donald E. Woessner 

Nobil Research & Devet. 

137"/THiclway Rd. 

Dallas, TX 75244 

Atan golfson 


Manning Park 


Denver D. Werstler 

GenCorp Research 

2990 Gitchrist Rd. 


Roger W. Wheattey 

Phospho Energetics Inc. 

3401 Market St. 


Carol F. Wichmann 

Merck & Co. R80R-203 

PO Box 2000 


Gerald D. Williams 

Penn St./Hershey Ned 



Even Williams 


611Hansen Way 


William K. Wilson 

Rice University 

Biochemistry 

PO Box 1892 


At Witunowski 


611Hansen Way 


Sue C. Witt 

WRRC 


Albany, CA 94710 

Roger A. Wolfe 

Occidental Chemical Corp. 

Technology Center 

Long Road 

Grand Island, NY 14072 

Tuck C. Wong 

University of Missouri 


Columbia, MO 65211

Warner R. Wootfenden 


Box 92 HE B[dg 



John M. Wright 


Dept of Chemistry B-014 

La Jotla, CA 92093 

Kurt Wuthrich 

ETH-Honggerberg 

lnst.Motekutahbiotogie 

und Biophysik 

CH8093, Zurich Switzerlnd 

Ching Yao 


533 Cabot Rd. 


Chin Yu 

Nat'[ Tsing Hua Univ. 


Hsinchu, 

Taiwart30043 Rep China 

Dieter Ziessow 

Technical Univ. Berlin 

I.N. Stranski Inst. 

Str 17 Juni 112,D1000 

Berlin 12, Germany 

Jan B. Wooten 

Phittip Norris Res & Dev 

PO Box 26583 

Richmond, VA 23261 

David A. Wright 




Ping Pin Yang 

Int'l Mineral & Chem Corp. 

PO Box 207 

Terre Haute, IN 47808 

James P. Yesinowski 

California lnst Tech 

MC 164-30 


Toby Zens 


611Hansen Way 


Eric R.P. Zuiderweg 

Abbott Labs 

NMR Research 


Denise L. Worthen 

Cattech 127-72 


Peter E. Wright 

Research Inst of 

Scripps Clinic 

Dept of Molecular Biology 


Constantino S. Yannoni 

IBM Almaden Res. 1(341802 

650 Harry Road 

San Jose, CA 95120-6099 

Hon9 N. Yeung 

4829 Lindsey (]vat 

Richmond Hgts., OH 44143 

Ning Zhou 

Univ. California 

Pharmaceutical ChemOept. 


Nicholas Zumbutyadis 


Research Labs 

Rochester, NY 14650

Notes

th  - 1987 - 51st ENC Conference

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