Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
- 1 December 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 100 (26), 8041-8047
- https://doi.org/10.1021/ja00494a001
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
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- Nuclear magnetic resonance investigation of nitrogen-15-labeled histidine in aqueous solutionJournal of the American Chemical Society, 1977
- Titration behavior and tautomeric states of individual histidine residues of myoglobins. Application of natural abundance carbon 13 nuclear magnetic resonance spectroscopy.Journal of Biological Chemistry, 1977
- Model for “charge-relay”: Acceleration by carboxylate anion in intramolecular general base-catalyzed ester hydrolysis by the imidazolyl groupProceedings of the National Academy of Sciences, 1977
- Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transferBiochemistry, 1976
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1968
- Three-dimensional Structure of Tosyl-α-chymotrypsinNature, 1967