Optimization and validation of multi-state NMR protein structures using structural correlations.

ABSTRACT: Recent advances in the field of protein structure determination using liquid-state NMR enable the elucidation of multi-state protein conformations that can provide insight into correlated and non-correlated protein dynamics at atomic resolution. So far, NMR-derived multi-state structures were typically evaluated by means of visual inspection of structure superpositions, target function values that quantify the violation of experimented restraints and root-mean-square deviations that quantify similarity between conformers. As an alternative or complementary approach, we present here the use of a recently introduced structural correlation measure, PDBcor, that quantifies the clustering of protein states as an additional measure for multi-state protein structure analysis. It can be used for v

SUBMITTER: Ashkinadze D 

PROVIDER: S-EPMC9018667 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature