Water Determines the Structure and Dynamics of Proteins

Chem Rev. 2016 Jul 13;116(13):7673-97. doi: 10.1021/acs.chemrev.5b00664. Epub 2016 May 17.


Water is an essential participant in the stability, structure, dynamics, and function of proteins and other biomolecules. Thermodynamically, changes in the aqueous environment affect the stability of biomolecules. Structurally, water participates chemically in the catalytic function of proteins and nucleic acids and physically in the collapse of the protein chain during folding through hydrophobic collapse and mediates binding through the hydrogen bond in complex formation. Water is a partner that slaves the dynamics of proteins, and water interaction with proteins affect their dynamics. Here we provide a review of the experimental and computational advances over the past decade in understanding the role of water in the dynamics, structure, and function of proteins. We focus on the combination of X-ray and neutron crystallography, NMR, terahertz spectroscopy, mass spectroscopy, thermodynamics, and computer simulations to reveal how water assist proteins in their function. The recent advances in computer simulations and the enhanced sensitivity of experimental tools promise major advances in the understanding of protein dynamics, and water surely will be a protagonist.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Hydrogen Bonding
  • Hydrostatic Pressure
  • Ion Channels / chemistry
  • Molecular Structure
  • Muramidase / chemistry
  • Phase Transition
  • Protein Denaturation
  • Proteins / chemistry*
  • Temperature
  • Terahertz Spectroscopy / methods
  • Water / chemistry*


  • Ion Channels
  • Proteins
  • Water
  • Muramidase