Abstract
The dynamical behaviour of four solid polypeptides (α-chymotrypsin, insulin, lysozyme, ribonuclease A) has been investigated by proton magnetic relaxation. The interpretation was supplemented by measurements on the constituent amino acids, and on dipeptides, tripeptides and homopolypeptides. The following motions were identified and characterized: methyl group reorientation, segmental motion, sidechain motion, proline ring puckering, reorientation of water molecules in the structure. Slow motions were investigated through measurements of the dipolar relaxation time T ID.
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