Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.

ABSTRACT: Protein structures are not static but sample different conformations over a range of amplitudes and time scales. These fluctuations may involve relatively small changes in bond angles or quite large rearrangements in secondary structure and tertiary fold. The equilibrium between discrete structural substates on the microsecond to millisecond time scale is sometimes termed conformational exchange. Protein dynamics and conformational exchange are believed to provide the basis for many important activities, such as protein-protein and protein-ligand interactions, enzymatic activity and protein allostery; however, for many proteins, the dynamics and conformational exchange that lead to function are poorly defined. Spectroscopic methods, such as NMR, are among the most important methods to expl

SUBMITTER: Cafiso DS 

PROVIDER: S-EPMC4204925 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature