Ontology highlight
ABSTRACT:
SUBMITTER: Marsh JA
PROVIDER: S-EPMC3145976 | biostudies-literature | 2011 Jun
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20110601 6
Protein interactions are often accompanied by significant changes in conformation. We have analyzed the relationships between protein structures and the conformational changes they undergo upon binding. Based upon this, we introduce a simple measure, the relative solvent accessible surface area, which can be used to predict the magnitude of binding-induced conformational changes from the structures of either monomeric proteins or bound subunits. Applying this to a large set of protein complexes ...[more]