SRLS Analysis of 15N–1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy
Author:
Affiliation:
1. The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 5290002, Israel
Funder
United States-Israel Binational Science Foundation
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.0c10124
Reference50 articles.
1. NMR Characterization of the Dynamics of Biomacromolecules
2. New Tools Provide New Insights in NMR Studies of Protein Dynamics
3. The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation
4. Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional Consequences
5. Dynamics of biomolecules from picoseconds to seconds at atomic resolution
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