Nuclear magnetic resonance study of the state of protonation of inhibitors bound to mutant dihydrofolate reductase lacking the active-site carboxyl
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00370a069
Reference29 articles.
1. Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding.
2. Inhibition of dihydrofolate reductase: effect of NADPH on the selectivity and affinity of diaminobenzylpyrimidines
3. Proton, carbon-13, and phosphorus-31 nuclear magnetic resonance studies of the dihydrofolate reductase-NADP-folate complex: characterization of three coexisting conformational states
4. Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP complex
5. Binding of methotrexate to dihydrofolate reductase and its relation to protonation of the ligand
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