Comparing interfacial dynamics in protein-protein complexes: an elastic network approach.

ABSTRACT:

Background

The transient, or permanent, association of proteins to form organized complexes is one of the most common mechanisms of regulation of biological processes. Systematic physico-chemical studies of the binding interfaces have previously shown that a key mechanism for the formation/stabilization of dimers is the steric and chemical complementarity of the two semi-interfaces. The role of the fluctuation dynamics at the interface of the interacting subunits, although expectedly important, proved more elusive to characterize. The aim of the present computational study is to gain insight into salient dynamics-based aspects of protein-protein interfaces.

Results

The interface dynamics was characterized by means of an elastic network model for 22 representative dimers cove

SUBMITTER: Zen A 

PROVIDER: S-EPMC2927602 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature