Proximity of two tryptophan residues in dihydrofolate reductase determined by 19F NMR
- 1 January 1978
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 271 (5641), 184-185
- https://doi.org/10.1038/271184a0
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- 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
- Selectively enriched [γ-13C]-histidine as a nuclear magnetic resonance probe of enzyme structure and function. Synthesis and incorporation into E.coli alkaline phosphataseBiochemical and Biophysical Research Communications, 1976
- Conformation and cooperativity in hemoglobinBiochemistry, 1975
- 19F nuclear magnetic resonance studies of structure and function relations in trifluoroacetonylated rabbit muscle glyceraldehyde-3-phosphate dehydrogenaseBiochemistry, 1975
- Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteasesBiochemistry, 1973
- An NMR method for characterizing conformation changes in proteinsBiochemical and Biophysical Research Communications, 1972
- N‐Fluoroacetyl‐d‐glucosamine as a Molecular Probe of Lysozyme StructureEuropean Journal of Biochemistry, 1971
- 19F magnetic resonance spectroscopic investigation of the binding of 2-deoxy-2-trifluoroacetamido-α-D-glucose to lysozymeJournal of the Chemical Society D: Chemical Communications, 1971
- Nuclear Magnetic Resonance Spectroscopy of Amino Acids, Peptides, and ProteinsAdvances in protein chemistry, 1970
- High-Resolution Nuclear Magnetic Resonance Spectra of Selectively Deuterated Staphylococcal NucleaseScience, 1968