Ligand-Dependent Conformational Dynamics of Dihydrofolate Reductase
Author:
Affiliation:
1. Department of Chemistry, Emory University, Atlanta, Georgia 30322, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b01364
Reference47 articles.
1. Toward an Understanding of the Role of Dynamics on Enzymatic Catalysis in Lactate Dehydrogenase
2. The Dynamical Nature of Enzymatic Catalysis
3. A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis
4. Evidence for a Functional Role of the Dynamics of Glycine-121 of Escherichia coli Dihydrofolate Reductase Obtained from Kinetic Analysis of a Site-Directed Mutant
5. Multiple Intermediates, Diverse Conformations, and Cooperative Conformational Changes Underlie the Catalytic Hydride Transfer Reaction of Dihydrofolate Reductase
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1. Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase;2024-06-18
2. Synthesis, Biological Activity, and Molecular Dynamics Study of Novel Series of a Trimethoprim Analogs as Multi-Targeted Compounds: Dihydrofolate Reductase (DHFR) Inhibitors and DNA-Binding Agents;International Journal of Molecular Sciences;2021-04-01
3. Distal Regions Regulate Dihydrofolate Reductase-Ligand Interactions;Methods in Molecular Biology;2020-12-15
4. Site-Specific Tryptophan Labels Reveal Local Microsecond–Millisecond Motions of Dihydrofolate Reductase;Molecules;2020-08-22
5. High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP+;Acta Crystallographica Section D Structural Biology;2018-09-01
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