Large-Scale Study of Hydration Environments through Hydration Sites Academic Article uri icon

Overview

MeSH Major

  • Brain
  • Diabetes Mellitus, Type 2
  • Hypoglycemia
  • Hypoglycemic Agents
  • Magnetic Resonance Imaging

abstract

  • © 2019 American Chemical Society. Hydration sites are locations of interest to water and they can be used to classify the behavior of water around chemical motifs commonly found on the surface of proteins. Inhomogeneous fluid solvation theory (IFST) is a method for calculating hydration free-energy changes from molecular dynamics (MD) trajectories. In this paper, hydration sites are identified from MD simulations of 380 diverse protein structures. The hydration free energies of the hydration sites are calculated using IFST and distributions of these free-energy changes are analyzed. The results show that for some hydration sites near features conventionally regarded as attractive to water, such as hydrogen bond donors, the water molecules are actually relatively weakly bound and are easily displaced. We also construct plots of the spatial density of hydration sites with high, medium, and low hydration free-energy changes which represent weakly and strongly bound hydration sites. It is found that these plots show consistent features around common polar amino acids for all of the proteins studied.

publication date

  • May 16, 2019

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1021/acs.jpcb.9b02490

Additional Document Info

start page

  • 4220

end page

  • 4229

volume

  • 123

number

  • 19