The Exact NOE as an Alternative in Ensemble Structure Determination.

ABSTRACT: The structure-function paradigm is increasingly replaced by the structure-dynamics-function paradigm. All protein activity is steered by the interplay between enthalpy and entropy. Conformational dynamics serves as a proxy of conformational entropy. Therefore, it is essential to study not only the average conformation but also the spatial sampling of a protein on all timescales. To this purpose, we have established a protocol for determining multiple-state ensembles of proteins based on exact nuclear Overhauser effects (eNOEs). We have recently extended our previously reported eNOE data set for the protein GB3 by a very large set of backbone and side-chain residual dipolar couplings and three-bond J couplings. Here, we demonstrate that at least four structural states are required to repres

SUBMITTER: Vogeli B 

PROVIDER: S-EPMC4806187 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature