Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.

ABSTRACT: The understanding of protein evolution depends on the ability to relate the impact of mutations on molecular traits to organismal fitness. Biological activity and robustness have been regarded as important features in shaping protein evolutionary landscapes. Conformational dynamics, which is essential for protein function, has received little attention in the context of evolutionary analyses. Here we employ NMR spectroscopy, the chief experimental tool to describe protein dynamics at atomic level in solution at room temperature, to study the intrinsic dynamic features of a metallo- Β: -lactamase enzyme and three variants identified during a directed evolution experiment that led to an expanded substrate profile. We show that conformational dynamics in the catalytically relevant microsecond

SUBMITTER: Gonzalez MM 

PROVIDER: S-EPMC5854100 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature