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Water Determines the Structure and Dynamics of Proteins
CEA Saclay, CNRS, Lab Leon Brillouin, F-91191 Gif Sur Yvette, France..
Abdus Salaam Int Ctr Theoret Phys, Condensed Matter & Stat Phys, I-34151 Trieste, Italy..
Ruhr Univ Bochum, Fac Chem & Biochem, Univ Str 150 Bldg NC 7-72, D-44780 Bochum, Germany..
Univ Manchester, Manchester Inst Biotechnol, 131 Princess St, Manchester M1 7DN, Lancs, England..
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2016 (English)In: Chemical Reviews, ISSN 0009-2665, E-ISSN 1520-6890, Vol. 116, no 13, 7673-7697 p.Article, review/survey (Refereed) PublishedText
Abstract [en]

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.

Place, publisher, year, edition, pages
2016. Vol. 116, no 13, 7673-7697 p.
National Category
Organic Chemistry
URN: urn:nbn:se:uu:diva-300654DOI: 10.1021/acs.chemrev.5b00664ISI: 000379794000011PubMedID: 27186992OAI: oai:DiVA.org:uu-300654DiVA: diva2:951849
The Royal Swedish Academy of SciencesSwedish Research Council
Available from: 2016-08-10 Created: 2016-08-10 Last updated: 2016-08-10Bibliographically approved

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