Fluorine-19 nuclear magnetic resonance studies of ligand binding to 3-fluorotyrosine- and 6-fluorotryptophan-containing dihydrofolate reductase from Lactobacillus casei
- 26 July 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (15), 3492-3500
- https://doi.org/10.1021/bi00634a032
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- 1 H nuclear magnetic resonance studies of Lactobacillus casei dihydrofolate reductase: effects of substrate and inhibitor binding on the histidine residuesProceedings of the Royal Society of London. B. Biological Sciences, 1977
- 1 H nuclear magnetic resonance studies of the tyrosine residues of selectively deuterated Lactobacillus casei dihydrofolate reductaseProceedings of the Royal Society of London. B. Biological Sciences, 1977
- Large-scale purification and characterization of dihydrofolate reductase from a methotrexate-resistant strain of Lactobacillus caseiBiochemical Journal, 1976
- Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate bindingBiochemistry, 1976