Protein motions and the activation of the CH bond catalyzed by dihydrofolate reductase
Author:
Funder
NSF
NIH
Publisher
Elsevier BV
Subject
Biochemistry,Analytical Chemistry
Reference45 articles.
1. Preservation of protein dynamics in dihydrofolate reductase evolution;Francis;J Biol Chem,2013
2. Extension and limits of the network of coupled motions correlated to hydride transfer in dihydrofolate reductase;Singh;J Am Chem Soc,2014
3. Probing coupled motions in enzymatic hydrogen tunnelling reactions;Allemann;Biochem Soc Trans,2009
4. Relating protein motion to catalysis;Hammes-Schiffer;Annu Rev Biochem,2006
5. Flexibility, diversity, and cooperativity: pillars of enzyme catalysis;Hammes;Biochemistry,2011
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1. Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase;2024-06-18
2. Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism;Proceedings of the National Academy of Sciences;2024-02-22
3. Resolving conformational changes that mediate a two-step catalytic mechanism in a model enzyme;2023-06-03
4. Evolution of Optimized Hydride Transfer Reaction and Overall Enzyme Turnover in Human Dihydrofolate Reductase;Biochemistry;2021-12-07
5. Role of Active Site Loop Dynamics in Mediating Ligand Release from E. coli Dihydrofolate Reductase;Biochemistry;2021-08-24
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