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th  - 1987 - 51st ENC Conference

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WF14<br />

THE USE OF MULTIPLE ECHO ACQUISITION AND STIMULATED ECHO5<br />

TO DETECT SLOW MOTIONS<br />

S. D. Kennedy, S. Ganapa<strong>th</strong>y, S. Swanson, R. 8. Bryant<br />

Department of Biophysics<br />

University of Rochester Medical Center<br />

Rochester, New York 14642<br />

The use of Fourier transformed echo trains was described by<br />

Zilm at <strong>th</strong>e <strong>ENC</strong> last year. The advantages for a number of<br />

studies include increases in signal to noise, clear<br />

demonstration of heterogeneous broadening, transverse<br />

relaxation time measurements rapidly, as well as sensitivity<br />

to motions of <strong>th</strong>e spins various types. We have demonstrated<br />

<strong>th</strong>at <strong>th</strong>e me<strong>th</strong>od provides a very efficient monitor of ms<br />

motions in polymers. The techniques are equally well suited<br />

to <strong>th</strong>e study of chemical exchange in <strong>th</strong>e solid or spin<br />

exchanges caused by relaxation. In <strong>th</strong>e basic spin echo train<br />

e~:periment, <strong>th</strong>e time scale limitation i~ imposed by <strong>th</strong>e<br />

effective transverse relaxation times in <strong>th</strong>e system~ which<br />

may vary considerably from sample to sample, but are<br />

typically in <strong>th</strong>e tens of ms range.<br />

The basic e~periment may be e~:tended in time by using a<br />

stimulated echo. The spins are phase encoded during <strong>th</strong>e<br />

period ÷ollowing <strong>th</strong>e 90 degree pulse or magnetization cycle<br />

by Hartmann-Hahn contact for example, <strong>th</strong>en stored along z for<br />

a variable time during which motion or a magnetic or chemical<br />

exchange event may change <strong>th</strong>e Larmor frequency. The read-out<br />

is accomplished wi<strong>th</strong> a <strong>th</strong>ird 90 degree pulse and <strong>th</strong>e<br />

formation of a stimulated echo. This experiment extends <strong>th</strong>e<br />

time scale of <strong>th</strong>e motion observation to <strong>th</strong>e carbon T, ra<strong>th</strong>er<br />

<strong>th</strong>an <strong>th</strong>e T2. We have applied <strong>th</strong>is technique in a series of<br />

polymers to detect slow motions. In molecules containing<br />

nitrogen such as peptides~ <strong>th</strong>e "4N may complicate<br />

interpretation of <strong>th</strong>e data in terms of motions alone. The<br />

e~:periment, when combined wi<strong>th</strong> o<strong>th</strong>er rela~:ation time<br />

measurements and MASS~ provides an easy me<strong>th</strong>od for measuring<br />

<strong>th</strong>e "4N T~, a parameter of interest in its own right. We<br />

report results on a series of amino acids and peptides <strong>th</strong>at<br />

demonstrates <strong>th</strong>e me<strong>th</strong>od and indicates <strong>th</strong>e importance of<br />

nitrogen relaxation times in dynamical intrepretations.

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