Probing the Role of an Active Site Aspartic Acid in Dihydrofolate Reductase
Author:
Affiliation:
1. Contribution from the Departments of Chemistry and Biology, University of Virginia, Charlottesville, Virginia, 22901, and Division of Biology, California Institute of Technology, Pasadena, California, 91125
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja971099l
Reference71 articles.
1. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
2. Dihydrofolate reductase
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