Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles.

ABSTRACT: Allostery describes altered protein function at one site due to a perturbation at another site. One mechanism of allostery involves correlated motions, which can occur even in the absence of substantial conformational change. We present a novel method, "MutInf", to identify statistically significant correlated motions from equilibrium molecular dynamics simulations. Our approach analyzes both backbone and sidechain motions using internal coordinates to account for the gear-like twists that can take place even in the absence of the large conformational changes typical of traditional allosteric proteins. We quantify correlated motions using a mutual information metric, which we extend to incorporate data from multiple short simulations and to filter out correlations that are not statisticall

SUBMITTER: McClendon CL 

PROVIDER: S-EPMC2790287 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature