Enthalpic Breakdown of Water Structure on Protein Active-Site Surfaces.

ABSTRACT: The principles underlying water reorganization around simple nonpolar solutes are well understood and provide the framework for the classical hydrophobic effect, whereby water molecules structure themselves around solutes so that they maintain favorable energetic contacts with both the solute and the other water molecules. However, for certain solute surface topographies, water molecules, due to their geometry and size, are unable to simultaneously maintain favorable energetic contacts with both the surface and neighboring water molecules. In this study, we analyze the solvation of ligand-binding sites for six structurally diverse proteins using hydration site analysis and measures of local water structure, in order to identify surfaces at which water molecules are unable to structure them

SUBMITTER: Haider K 

PROVIDER: S-EPMC5009012 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature