Evolution Conserves the Network of Coupled Residues in Dihydrofolate Reductase
Author:
Affiliation:
1. Department of Chemistry, The University of Iowa, Iowa City, Iowa 52242, United States
2. Department of Biochemistry & Cellular and Molecular Biology, The University of Tennessee, Knoxville, Knoxville, Tennessee 37996, United States
Funder
Division of Chemistry
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00460
Reference53 articles.
1. Functionally Important Conformations of the Met20 Loop in Dihydrofolate Reductase are Populated by Rapid Thermal Fluctuations
2. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
3. Barrier crossing in dihydrofolate reductase does not involve a rate-promoting vibration
4. Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
5. Hydrogen Tunneling Links Protein Dynamics to Enzyme Catalysis
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1. Evolution of Optimized Hydride Transfer Reaction and Overall Enzyme Turnover in Human Dihydrofolate Reductase;Biochemistry;2021-12-07
2. Capturing the Catalytic Proton of Dihydrofolate Reductase: Implications for General Acid–Base Catalysis;ACS Catalysis;2021-04-28
3. Electrostatic Switching Controls Channel Dynamics of the Sensor Protein VirB10 in A. tumefaciens Type IV Secretion System;ACS Omega;2020-02-04
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