Volume-based solvation models out-perform area-based models in combined studies of wild-type and mutated protein-protein interfaces.

ABSTRACT:

Background

Empirical binding models have previously been investigated for the energetics of protein complexation (DeltaG models) and for the influence of mutations on complexation (i.e. differences between wild-type and mutant complexes, DeltaDeltaG models). We construct binding models to directly compare these processes, which have generally been studied separately.

Results

Although reasonable fit models were found for both DeltaG and DeltaDeltaG cases, they differ substantially. In a dataset curated for the absence of mainchain rearrangement upon binding, non-polar area burial is a major determinant of DeltaG models. However this DeltaG model does not fit well to the data for binding differences upon mutation. Burial of non-polar area is weighted down in fitting of DeltaDe

SUBMITTER: Bougouffa S 

PROVIDER: S-EPMC2596146 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature