Abstract
Measurements have been made of the proton NMR spin-lattice relaxation at 60, 30 and 18 MHz in solid ribonuclease A from 10 to 300 K, and in α-chymotrypsin, lysozyme and deuterated lysozyme from 120 to 300 K. Reorientation of the methyl groups is the predominant molecular motion causing relaxation. A lognormal distribution of correlation times best characterizes the motions, with a spread of activation energies 14 ± 6 kJ mole .
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