Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine
- 14 August 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 281 (2) , 323-339
- https://doi.org/10.1006/jmbi.1998.1935
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Structure, Catalytic Mechanism, and Evolution of the Glutathione TransferasesChemical Research in Toxicology, 1997
- Real-Time Refolding Studies of 6-19F-Tryptophan Labeled Escherichia coli Dihydrofolate Reductase Using Stopped-Flow NMR SpectroscopyBiochemistry, 1996
- Mechanism of the Reaction Catalyzed by .DELTA.5-3-Ketosteroid Isomerase of Comamonas (Pseudomonas) testosteroni: Kinetic Properties of a Modified Enzyme in Which Tyrosine 14 Is Replaced by 3-FluorotyrosineBiochemistry, 1994
- Conformational differences between complexes of elongation factor Tu studied by 19F‐NMR spectroscopyEuropean Journal of Biochemistry, 1993
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- A fast algorithm for rendering space-filling molecule picturesJournal of Molecular Graphics, 1988
- Structure and refinement of penicillopepsin at 1.8 Å resolutionJournal of Molecular Biology, 1983
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- 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
- Fluorotyrosine alkaline phosphatase. Fluorine-19 nuclear magnetic resonance relaxation times and molecular motion of the individual fluorotyrosinesBiochemistry, 1974