The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate
- 15 October 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 272 (1-2), 34-36
- https://doi.org/10.1016/0014-5793(90)80442-l
Abstract
Growth of Escherichia coli in the presence of glyphosate, an inhibitor of aromatic amino acid biosynthesis, has permitted the production of proton translocating ATPase that is specifically labelled with 5-fluorotryptophan. Five sets of 19F nuclear magnetic resonances are resolved. The use of glyphosphate should be of wide applicability in the preparation of proteins labelled in aromatic amino acid residues for NMR studies.Keywords
This publication has 22 references indexed in Scilit:
- Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromoleculesQuarterly Reviews of Biophysics, 1990
- Biosynthetic Incorporation of15N and13C for Assignment and Interpretation of Nuclear Magnetic Resonance Spectra of ProteinsQuarterly Reviews of Biophysics, 1990
- Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coliBiochemistry, 1987
- Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondriaJournal of Molecular Biology, 1985
- Fluorine-19 nuclear magnetic resonance study of 5-fluorotryptophan-labeled histidine-binding protein J of Salmonella typhimuriumJournal of Molecular Biology, 1984
- Functional groups at the catalytic site of F1 adenosine triphosphataseBiochemistry, 1980
- The uncA gene codes for the α-subunit of the adenosine triphosphatase of Escherichia coli. Electrophoretic analysis of uncA mutant strainsBiochemical Journal, 1979
- Fluorine-19 nuclear magnetic resonance studies of ligand binding to 3-fluorotyrosine- and 6-fluorotryptophan-containing dihydrofolate reductase from Lactobacillus caseiBiochemistry, 1977
- Fluorotyrosine Alkaline Phosphatase from Escherichia coli : Preparation, Properties, and Fluorine-19 Nuclear Magnetic Resonance SpectrumProceedings of the National Academy of Sciences, 1974
- Study of cooperative interactions in hemoglobin using fluorine nuclear magnetic resonanceBiochemistry, 1972