Abstract
A novel formalism for estimating the complex motions of proteins and other flexible macromolecules from NMR relaxation measurements is applied to 13C NMR relaxation data on the Bovine Pancreatic Trypsin Inhibitor (M. W. 6,500). Six experimental parameters measured at two field strengths are accounted for by a minimum of three motions at each carbon group. Low frequency components make small but finite contribution to the relaxation of all resonances, suggesting a general low frequency distortion of the backbone. Rotational diffusion of the protein makes a relatively minor contribution to the relaxation process. For aliphatic groups, rotation of side chains dominates relaxation.
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