Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase.

ABSTRACT: Enzymes are known to change among several conformational states during turnover. The role of such dynamic structural changes in catalysis is not fully understood. The influence of dynamics in catalysis can be inferred, but not proven, by comparison of equilibrium structures of protein variants and protein-ligand complexes. A more direct way to establish connections between protein dynamics and the catalytic cycle is to probe the kinetics of specific protein motions in comparison to progress along the reaction coordinate. We have examined the enzyme model system dihydrofolate reductase (DHFR) from Escherichia coli with tryptophan fluorescence-probed temperature-jump spectroscopy. We aimed to observe the kinetics of the ligand binding and ligand-induced conformational changes of three DHFR c

SUBMITTER: Reddish MJ 

PROVIDER: S-EPMC4806677 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature