Use of the neutron diffraction--H/D exchange technique to determine the conformational dynamics of trypsin.

Abstract

A number of structural and chemical investigations (1–6) have shown that, even though protein molecules possess a high degree of secondary structure, they have numerous component segments which exhibit substantial fluctuations from their native conformations. A majority of these fluctuations represent a localized denaturation of small portions of the structure and result from the natural equilibrium between protein-protein and protein-solvent interactions. Although most of these fluctuations probably have little direct effect on the regions responsible for functional activity of the protein, a growing body of evidence indicates that conformational change is an important ingredient in a significant number of biological processes (7–10).