A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family.

ABSTRACT: Conformational ensembles are increasingly recognized as a useful representation to describe fundamental relationships between protein structure, dynamics and function. Here we present an ensemble of ubiquitin in solution that is created by sampling conformational space without experimental information using "Backrub" motions inspired by alternative conformations observed in sub-Angstrom resolution crystal structures. Backrub-generated structures are then selected to produce an ensemble that optimizes agreement with nuclear magnetic resonance (NMR) Residual Dipolar Couplings (RDCs). Using this ensemble, we probe two proposed relationships between properties of protein ensembles: (i) a link between native-state dynamics and the conformational heterogeneity observed in crystal structures, and

SUBMITTER: Friedland GD 

PROVIDER: S-EPMC2682763 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature