Hydrogen-bond dynamics at the bio–water interface in hydrated proteins: a molecular-dynamics study-Reference-Cited by-同舟云学术

Hydrogen-bond dynamics at the bio–water interface in hydrated proteins: a molecular-dynamics study

Published:2017 Issue:1 Volume:19 Page:318-329
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Nandi Prithwish K.¹²³⁴,English Niall J.¹²³⁴,Futera Zdenek¹²³⁴,Benedetto Antonio⁵²³⁴⁶

Affiliation:

1. School of Chemical and Bioprocess Engineering

2. University College Dublin

3. Dublin 4

4. Ireland

5. School of Physics

6. Neutron-Scattering and Imaging Laboratory

Abstract

Hydration water's dynamical-crossover lies not at the origin of the protein residues' larger-amplitude motions, but rather arises as a consequence thereof.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CP/C6CP05601F

Reference61 articles.

1. J. A. Rupley and G.Careri, in Advances in Protein Chemistry, ed. C. B. Anfinsen, J. T. Edsall, F. M. Richards and D. S. Eisenberg, Academic Press, Cambridge, 1991, vol. 41, pp. 37–172

2. Crystalline ribonuclease A loses function below the dynamical transition at 220 K

3. Microscopic origins of entropy, heat capacity and the glass transition in proteins

4. Bulk-solvent and hydration-shell fluctuations, similar to - and -fluctuations in glasses, control protein motions and functions

5. Proteins in action: the physics of structural fluctuations and conformational changes

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