title: Water Determines the Structure and Dynamics of Proteins.
abstract: 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.
authors.affiliation: Laboratoire Léon Brillouin (CEA-CNRS) CEA Saclay F-91191 Gif Sur Yvette, France.
authors.forename: Marie-Claire
authors.initials: MC
authors.lastname: Bellissent-Funel
authors.affiliation: International Center for Theoretical Physics, Condensed Matter and Statistical Physics 34151 Trieste, Italy.
authors.forename: Ali
authors.initials: A
authors.lastname: Hassanali
authors.affiliation: Ruhr-Universität Bochum , Faculty of Chemistry and Biochemistry Universitätsstraße 150 Building NC 7/72, D-44780 Bochum, Germany.
authors.forename: Martina
authors.initials: M
authors.lastname: Havenith
authors.affiliation: Manchester Institute of Biotechnology The University of Manchester , 131 Princess Street, Manchester M1 7DN, United Kingdom.
authors.forename: Richard
authors.initials: R
authors.lastname: Henchman
authors.affiliation: Johannes Kepler University , Gruberstrasse, 40 4020 Linz, Austria.
authors.forename: Peter
authors.initials: P
authors.lastname: Pohl
authors.affiliation: Institut de Biologie Physico-Chimique Laboratoire de Biochimie Théorique 13 Rue Pierre et Marie Curie, 75005 Paris, France.
authors.forename: Fabio
authors.initials: F
authors.lastname: Sterpone
authors.affiliation: Department of Cell and Molecular Biology, Computational and Systems Biology, Uppsala University , 751 24 Uppsala, Sweden.
authors.forename: David
authors.initials: D
authors.lastname: van der Spoel
authors.affiliation: Ruhr-Universität Bochum , Faculty of Chemistry and Biochemistry Universitätsstraße 150 Building NC 7/72, D-44780 Bochum, Germany.
authors.forename: Yao
authors.initials: Y
authors.lastname: Xu
authors.affiliation: Center for Non Linear Studies, Los Alamos National Laboratory , Los Alamos, New Mexico 87545, United States.
authors.forename: Angel E
authors.initials: AE
authors.lastname: Garcia
mesh_terms: D006860:Hydrogen Bonding; D006874:Hydrostatic Pressure; D007473:Ion Channels / Q000737:chemistry; D015394:Molecular Structure; D009113:Muramidase / Q000737:chemistry; D044367:Phase Transition; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D055068:Terahertz Spectroscopy / Q000379:methods; D014867:Water / Q000737:chemistry*
chemical_list: D007473:Ion Channels; D011506:Proteins; D014867:Water; D009113:Muramidase