Motion at the active site of [(4-fluorophenyl)sulfonyl]chymotrypsin
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00365a008
Reference40 articles.
1. Fluorine magnetic resonance studies of fluorine-substituted benzoyl chymotrypsins
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3. Irreversible enzyme inhibitors. CXLIX. Tissue-specific irreversible inhibitors of dihydrofolic reductase
4. Becker, E. D. (1980) High-Resolution NMR, 2nd ed., p74, Academic, New York.
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1. Advancing Biocatalysis through Enzyme, Cellular, and Platform Engineering;Biotechnology Progress;2008-06-06
2. Fluorine NMR of proteins;Progress in Nuclear Magnetic Resonance Spectroscopy;1994-01
3. NMR studies of the α-chymotrypsin-(R)-1-acetamido-2-(4-fluorophenyl)ethane-1-boronic acid complex;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1993-06
4. Examination of the structure and dynamics of tosylchymotrypsin at pH 4 by tritium NMR spectroscopy;Journal of the American Chemical Society;1993-04
5. Structure and dynamics of α-chymotrypsin-N-trifluoroacetyl-4-fluorophenylalanine complexes;Journal of Biomolecular Nmr;1991-07
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