Functionally Important Conformations of the Met20 Loop in Dihydrofolate Reductase are Populated by Rapid Thermal Fluctuations-Reference-Cited by-同舟云学术

Functionally Important Conformations of the Met20 Loop in Dihydrofolate Reductase are Populated by Rapid Thermal Fluctuations

Published:2009-03-26 Issue:15 Volume:131 Page:5642-5647
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Arora Karunesh¹,Brooks III Charles L.¹

Affiliation:

1. Department of Chemistry and Biophysics Program, University of Michigan, 930 North University Avenue, Ann Arbor, Michigan 48109

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9000135

Reference53 articles.

1. In search of dihydrofolate reductase

2. Blakely, R. L.InChemistry and Biochemistry of Folates. In folates and pterins;Blakely, R. L. and Benkovic, S. J., Eds.Wiley:New York, 1984; Vol.3, pp191−253.

3. Protein Dynamics in Enzymatic Catalysis: Exploration of Dihydrofolate Reductase

4. Network of coupled promoting motions in enzyme catalysis

5. How Dihydrofolate Reductase Facilitates Protonation of Dihydrofolate

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