Conformational kinetics reveals affinities of protein conformational states.

ABSTRACT: Most biological reactions rely on interplay between binding and changes in both macromolecular structure and dynamics. Practical understanding of this interplay requires detection of critical intermediates and determination of their binding and conformational characteristics. However, many of these species are only transiently present and they have often been overlooked in mechanistic studies of reactions that couple binding to conformational change. We monitored the kinetics of ligand-induced conformational changes in a small protein using six different ligands. We analyzed the kinetic data to simultaneously determine both binding affinities for the conformational states and the rate constants of conformational change. The approach we used is sufficiently robust to determine the affinitie

SUBMITTER: Daniels KG 

PROVIDER: S-EPMC4522757 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature