Methods of Experimental Physics: Biophysics by Harold Lecar

By Harold Lecar

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By Harold Lecar

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Packard, Phys. Rev. 69, 127 (1946). *E M . C. Pound, Phys. Rrr. 37 (1946) 1 METHODS OF EXPERIMkNTAI. , 20 Ciipyright @ 1982 hy Ac;idcmic Prc\*. iny limn r c w v e d ISBN 0-12-475062-9 2 1. NUCLEAR MAGNETIC RESONANCE one to sample the details of motional processes in molecules. Biophysics deals in part with the structure and dynamics of biological molecules and assemblies, especially those aspects which pertain to biological function. Biomolecular structure has received considerable attention in biological NMR in the past.

After the pulse is turned off, magnetic resonance is observed as the decay of the induced signal, called the free-induction decay (FID). Both the FID and the frequency spectrum contain the same F. Bloch, Phys. R w . , 70, 460 (1946). 1. 8 NUCLEAR MAGNETIC RESONANCE information characterizing the system under study. , the spectrum), it is more convenient. On the other hand, the FID (the time domain function) is obtained in a fraction of the time (10- 2-10- 3, necessary to acquire a frequency spectrum by the CW method.

Chem. 3. The Tls for these nuclei will then be a function of structural factors only, namely, the number and the gyromagnetic ratio of the nuclei coupled magnetically to the carbon atoms and the respective internuclear distances. Because of the low natural abundance of 13C (about 1%) and the strong r - 6 dependence of the relaxation rate, the only significant dipolar contribution to the 13C Tl should come from directly bonded protons, in which case the r values will be similar as well. Accordingly, we predict that Tl for the ring carbons should decrease with the number of protons bonded to them.

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