Reconstruction of Protein Side-Chain Conformational Free Energy Surfaces From NMR-Derived Methyl Axis Order Parameters-Reference-Cited by-同舟云学术

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Reconstruction of Protein Side-Chain Conformational Free Energy Surfaces From NMR-Derived Methyl Axis Order Parameters

Published:2012-03-26 Issue:14 Volume:116 Page:4124-4133
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Krishnan Marimuthu¹,Smith Jeremy C.²³

Affiliation:

1. Center for Computational Natural Sciences and Bioinformatics, International Institute of Information Technology, Hyderabad 500 032, India

2. University of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics, Oak Ridge, Tennessee 37831, United States

3. Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996, United States

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp2104853

Reference60 articles.

1. The Role of Dynamics in Enzyme Activity

2. Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution

3. Protein dynamics from NMR

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1. NMR studies of rotamers with multi-substituted amides;Journal of Engineering Sciences and Innovation;2021-11-17

2. Correlated Response of Protein Side-Chain Fluctuations and Conformational Entropy to Ligand Binding;The Journal of Physical Chemistry B;2021-08-23

3. Validating the CHARMM36m protein force field with LJ-PME reveals altered hydrogen bonding dynamics under elevated pressures;Communications Chemistry;2021-06-28

4. Measuring Entropy in Molecular Recognition by Proteins;Annual Review of Biophysics;2018-05-20

5. Direct Determination of Site-Specific Noncovalent Interaction Strengths of Proteins from NMR-Derived Fast Side Chain Motional Parameters;The Journal of Physical Chemistry B;2017-05-15

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