On the packing density of the unbound protein-protein interaction interface and its implications in dynamics.

ABSTRACT:

Background

Characterizing the interface residues will help shed light on protein-protein interactions, which are involved in many important biological processes. Many studies focus on characterizing sequence or structure features of protein interfaces, but there are few studies characterizing the dynamics of interfaces. Therefore, we would like to know whether there is any specific dynamics pattern in the protein-protein interaction interfaces. Thermal fluctuation is an important dynamical property for a residue, and could be quickly estimated by local packing density without large computation since studies have showen closely relationship between these two properties. Therefore, we divided surface of an unbound subunit (free protein subunits before they are involved in forming the

SUBMITTER: Lin JJ 

PROVIDER: S-EPMC4331706 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature