Toward a unified representation of protein structural dynamics in solution.

ABSTRACT: An atomic resolution description of protein flexibility is essential for understanding the role that structural dynamics play in biological processes. Despite the unique dependence of nuclear magnetic resonance (NMR) to motional averaging on different time scales, NMR-based protein structure determination often ignores the presence of dynamics, representing rapidly exchanging conformational equilibria in terms of a single static structure. In this study, we use the rich dynamic information encoded in experimental NMR parameters to develop a molecular and statistical mechanical characterization of the conformational behavior of proteins in solution. Critically, and in contrast to previously proposed techniques, we do not use empirical energy terms to restrain a conformational search, a proc

SUBMITTER: Markwick PR 

PROVIDER: S-EPMC2779067 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature