15N–H-Related Conformational Entropy Changes Entailed By Plexin-B1 RBD Dimerization: Combined Molecular Dynamics/NMR Relaxation Approach
Author:
Affiliation:
1. Department of Chemical Sciences, University of Padova, Padova 35131, Italy
2. The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel
Funder
Israel Science Foundation
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.7b01079
Reference44 articles.
1. Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein Folding
2. NMR Relaxation Studies of the Role of Conformational Entropy in Protein Stability and Ligand Binding
3. New Tools Provide New Insights in NMR Studies of Protein Dynamics
4. The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
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