Abstract

From Human Structural Disorders to Basic Physical Chemistry to Protein Dynamics, Folding and Misfolding

Author(s): Andrew Smith

Proteins can move in a variety of ways, including the rotation of the side chains of amino acids and the movement of large domains. Because of the conformational flexibility of proteins, it is believed that they can rapidly and dynamically switch between a varieties of conformational substates. This theory has received support from numerous experimental techniques and computer simulations of protein dynamics. Investigations of the subunit dissociation of oligomeric proteins driven by hydrostatic pressure suggest that the typical times for subunit exchange between oligomers and for interconversion between different conformations may be rather slow (hours or days). Instead of an ensemble of conformational substates that rapidly interconvert, proteins should be seen in this context as a consistently diversified population of various long lived conformers.