Structural Interface Forms and Their Involvement in Stabilization of Multidomain Proteins or Protein Complexes.

ABSTRACT: The presented analysis concerns the inter-domain and inter-protein interface in protein complexes. We propose extending the traditional understanding of the protein domain as a function of local compactness with an additional criterion which refers to the presence of a well-defined hydrophobic core. Interface areas in selected homodimers vary with respect to their contribution to share as well as individual (domain-specific) hydrophobic cores. The basic definition of a protein domain, i.e., a structural unit characterized by tighter packing than its immediate environment, is extended in order to acknowledge the role of a structured hydrophobic core, which includes the interface area. The hydrophobic properties of interfaces vary depending on the status of interacting domains-In this contex

SUBMITTER: Dygut J 

PROVIDER: S-EPMC5085769 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature