Thermodynamic Properties of Water Molecules at a Protein-Protein Interaction Surface.

ABSTRACT: Protein-protein interactions (PPIs) have been identified as a vital regulator of cellular pathways and networks. However, the determinants that control binding affinity and specificity at protein surfaces are incompletely characterized and thus unable to be exploited for the purpose of developing PPI inhibitors to control cellular pathways in disease states. One of the key factors in intermolecular interactions that remains poorly understood is the role of water molecules and in particular the importance of solvent entropy. This factor is expected to be particularly important at protein surfaces, and the release of water molecules from hydrophobic regions is one of the most important drivers of PPIs. In this work, we have studied the protein surface of a mutant of the protein RadA to quant

SUBMITTER: Huggins DJ 

PROVIDER: S-EPMC3924879 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature