Accurate Determination of Conformational Transitions in Oligomeric Membrane Proteins.

ABSTRACT: The structural dynamics governing collective motions in oligomeric membrane proteins play key roles in vital biomolecular processes at cellular membranes. In this study, we present a structural refinement approach that combines solid-state NMR experiments and molecular simulations to accurately describe concerted conformational transitions identifying the overall structural, dynamical, and topological states of oligomeric membrane proteins. The accuracy of the structural ensembles generated with this method is shown to reach the statistical error limit, and is further demonstrated by correctly reproducing orthogonal NMR data. We demonstrate the accuracy of this approach by characterising the pentameric state of phospholamban, a key player in the regulation of calcium uptake in the sarcopla

SUBMITTER: Sanz-Hernandez M 

PROVIDER: S-EPMC4791661 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature