Water Determines the Structure and Dynamics of Proteins
Year: 2016
Type: review
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.
Source: Chemical Reviews
Institutions: Centre National de la Recherche Scientifique, Commissariat à l'Énergie Atomique et aux Énergies Alternatives, Laboratoire Léon Brillouin, CEA Paris-Saclay, The Abdus Salam International Centre for Theoretical Physics (ICTP), Ruhr University Bochum, University of Manchester, Johannes Kepler University of Linz, Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, Uppsala University, Chinese Academy of Sciences, Los Alamos National Laboratory
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2395521783