Coincidence of Dynamical Transitions in a Soluble Protein and Its Hydration Water: Direct Measurements by Neutron Scattering and MD Simulations-Reference-Cited by-同舟云学术

Coincidence of Dynamical Transitions in a Soluble Protein and Its Hydration Water: Direct Measurements by Neutron Scattering and MD Simulations

Published:2008-03-14 Issue:14 Volume:130 Page:4586-4587
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Wood Kathleen¹,Frölich Andreas¹,Paciaroni Alessandro¹,Moulin Martine¹,Härtlein Michael¹,Zaccai Giuseppe¹,Tobias Douglas J.¹,Weik Martin¹

Affiliation:

1. Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale, Jean Pierre EBEL, 41 rue Jules Horowitz, F-38027 Grenoble; CEA; CNRS; Université Joseph Fourier, Dipartimento di Fisica, Universita' di Perugia, Via Pascoli, 06123 Perugia, Italy, Institut Laue-Langevin, 6 rue Jules Horowitz, B.P. 156, 38042 Grenoble Cedex 9, France, and Department of Chemistry, Center for Biomembrane Systems and Institute for Surface and Interface Science, University of California, Irvine, California

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja710526r

Reference27 articles.

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

2. Translational Hydration Water Dynamics Drives the Protein Glass Transition

3. Relaxation Processes in Supercooled Confined Water and Implications for Protein Dynamics

4. Controlling the Protein Dynamical Transition with Sugar-Based Bioprotectant Matrices: A Neutron Scattering Study

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