Relaxation and single site multiple mutations to identify and control allosteric networks-Reference-Cited by-同舟云学术

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Relaxation and single site multiple mutations to identify and control allosteric networks

Published:2023-08 Issue: Volume:216 Page:51-57
ISSN:1046-2023
Container-title:Methods
language:en
Short-container-title:Methods

Author:

Lee Eunjeong,Redzic Jasmina S.,Zohar Eisenmesser Elan

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology,Molecular Biology

Reference27 articles.

1. Allostery: An Overview of Its History, Concepts, Methods, and Applications;Liu;PLoS Comput Biol,2016

2. The dark energy of proteins comes to light: conformational entropy and its role in protein function revealed by NMR relaxation;Wand;Curr Opin Struct Biol,2013

3. Wand, A. J.; Moorman, V. R.; Harpole, K. W., A Surprising Role for Conformational Entropy in Protein Function. In Dynamics in Enzyme Catalysis, Klinman, J.; HammesSchiffer, S., Eds. 2013; Vol. 337, pp 69-94.

4. Protein flexibility and conformational entropy in ligand design targeting the carbohydrate recognition domain of galectin-3;Diehl;J Am Chem Soc,2010

5. The dynamic energy landscape of dihydrofolate reductase catalysis;Boehr;Science,2006

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Rheostats, toggles, and neutrals, Oh my! A new framework for understanding how amino acid changes modulate protein function;Journal of Biological Chemistry;2024-03

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