Conformational Entropy from Mobile Bond Vectors in Proteins: A Viewpoint that Unifies NMR Relaxation Theory and Molecular Dynamics Simulation Approaches-Reference-Cited by-同舟云学术

Conformational Entropy from Mobile Bond Vectors in Proteins: A Viewpoint that Unifies NMR Relaxation Theory and Molecular Dynamics Simulation Approaches

Published:2020-09-26 Issue:42 Volume:124 Page:9323-9334
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Mendelman Netanel¹,Zerbetto Mirco²^ORCID,Buck Matthias³,Meirovitch Eva¹^ORCID

Affiliation:

1. The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900 Israel

2. Department of Chemical Sciences, University of Padova, Padova 35131, Italy

3. Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio 44106, United States

Funder

United States-Israel Binational Science Foundation

Israel Science Foundation

National Institute of General Medical Sciences

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/acs.jpcb.0c05846

Reference49 articles.

1. NMR order parameters and free energy: an analytical approach and its application to cooperative calcium(2+) binding by calbindin D9k

2. Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein Folding

3. Insights into the local residual entropy of proteins provided by NMR relaxation

4. The role of backbone conformational heat capacity in protein stability: Temperature dependent dynamics of the B1 domain ofStreptococcalprotein G

5. Conformational dynamics and thermodynamics of protein–ligand binding studied by NMR relaxation

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