[13] Fluorine nuclear magnetic resonance studies of proteins
- 1 January 1978
- book chapter
- Published by Elsevier in Methods in Enzymology
- Vol. 49, 270-295
- https://doi.org/10.1016/s0076-6879(78)49015-9
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Characterization of concanavalin A sugar binding site by fluorine-19 nuclear magnetic resonanceBiochemistry, 1974
- Aromatic hydrophobes and β-lactoglobulin A. Kinetics of binding by nuclear magnetic resonanceBiochemistry, 1972
- Catalytic mechanism of pepsin using a new synthetic substrateBiochemistry, 1972
- Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to .alpha.-chymotrypsinJournal of the American Chemical Society, 1972
- Investigation of the mechanism of ligand binding with cobalt(II) human carbonic anhydrase by hydrogen-1 and fluorine-19 nuclear magnetic resonance spectroscopyBiochemistry, 1971
- 19F magnetic resonance spectroscopic investigation of the binding of N-trifluoroacetylated amino-acids by chymotrypsinJournal of the Chemical Society D: Chemical Communications, 1971
- Enzyme-inhibitor interactions studied via fluorine magnetic resonanceArchives of Biochemistry and Biophysics, 1970
- Application of transient nuclear magnetic resonance methods to the measurement of biological exchange rates. Interaction of trifluoroacetyl-D-phenylalanine with the chymotrypsinsJournal of the American Chemical Society, 1969
- Enzyme-inhibitor interactions studied via fluorine nuclear magnetic resonance. I. The interaction of α-chymotrypsin with DL-N-trifluoroacetylphenylalanineBiochemical and Biophysical Research Communications, 1968
- Enzyme-substrate interaction by nuclear magnetic resonanceJournal of the American Chemical Society, 1967