Identification of hot spot residues at protein-protein interface.

ABSTRACT: It is known that binding free energy of protein-protein interaction is mainly contributed by hot spot (high energy) interface residues. Here, we investigate the characteristics of hot spots by examining inter-atomic sidechain-sidechain interactions using a dataset of 296 alanine-mutated interface residues. Results show that hot spots participate in strong and energetically favorable sidechain-sidechain interactions. Subsequently, we describe a novel, yet simple 'hot spot' prediction model with an accuracy that is similar to many available approaches. The model is also shown to efficiently distinguish specific protein-protein interactions from non-specific interactions.

SUBMITTER: Li L 

PROVIDER: S-EPMC1891667 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature