Dynamics of Hydration Water Plays a Key Role in Determining the Binding Thermodynamics of Protein Complexes.

ABSTRACT: Interfacial waters are considered to play a crucial role in protein-protein interactions, but in what sense and why are they important? Here, using molecular dynamics simulations and statistical thermodynamic analyses, we demonstrate distinctive dynamic characteristics of the interfacial water and investigate their implications for the binding thermodynamics. We identify the presence of extraordinarily slow (~1,000 times slower than in bulk water) hydrogen-bond rearrangements in interfacial water. We rationalize the slow rearrangements by introducing the "trapping" free energies, characterizing how strongly individual hydration waters are captured by the biomolecular surface, whose magnitude is then traced back to the number of water-protein hydrogen bonds and the strong electrostatic fiel

SUBMITTER: Chong SH 

PROVIDER: S-EPMC5562873 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature