The Low-Temperature Inflection Observed in Neutron Scattering Measurements of Proteins Is Due to Methyl Rotation: Direct Evidence Using Isotope Labeling and Molecular Dynamics Simulations-Reference-Cited by-同舟云学术

The Low-Temperature Inflection Observed in Neutron Scattering Measurements of Proteins Is Due to Methyl Rotation: Direct Evidence Using Isotope Labeling and Molecular Dynamics Simulations

Published:2010-03-19 Issue:14 Volume:132 Page:4990-4991
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Wood Kathleen¹,Tobias Douglas J.¹,Kessler Brigitte¹,Gabel Frank¹,Oesterhelt Dieter¹,Mulder Frans A. A.¹,Zaccai Giuseppe¹,Weik Martin¹

Affiliation:

1. Institut Laue Langevin, Grenoble Cedex 9, France, Australian Nuclear Science and Technology Organisation, Menai NSW Australia, Department of Chemistry, University of California, Irvine, California, Max Planck Institute of Biochemistry, Martinsried, Germany, CEA, IBS, Laboratoire de Biophysique Moleculaire, F-38054 Grenoble, France, CNRS, UMR5075, F-38027, Grenoble, France, Universite Joseph Fourier, F-38000, Grenoble, France, Groningen Biomolecular Sciences and Biotechnology Institute, University of...

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja910502g

Reference29 articles.

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

2. Onsets of Anharmonicity in Protein Dynamics

3. Methyl Group Dynamics as a Probe of the Protein Dynamical Transition

4. What Contributions to Protein Side-chain Dynamics are Probed by NMR Experiments? A Molecular Dynamics Simulation Analysis

5. The Origin of Protein Sidechain Order Parameter Distributions

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