The pKa value of His 57-Asp 102 couple in the active site of bovine pancreatic β-trypsin: A molecular orbital study
- 1 December 1982
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 99 (4) , 759-775
- https://doi.org/10.1016/0022-5193(82)90196-5
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- THE CATALYTIC FUNCTION OF ACTIVE SITE AMINO ACID SIDE CHAINS IN WELL‐CHARACTERIZED ENZYMES*Annals of the New York Academy of Sciences, 1981
- Effect of electron correlation on theoretical equilibrium geometriesJournal of the American Chemical Society, 1979
- Molecular structure of the α-lytic protease from Myxobacter 495 at 2·8 Å resolutionJournal of Molecular Biology, 1979
- 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 proteasesJournal of the American Chemical Society, 1978
- Molecular Orbital studies on the Enzymatic Reaction Mechanism of Serine Proteases. I. Charge Relay System in Substrate Free StateJournal of the Physics Society Japan, 1977
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- The refined crystal structure of bovine β-trypsin at 1·8 Å resolutionJournal of Molecular Biology, 1975
- Tertiary structural differences between microbial serine proteases and pancreatic serine enzymesNature, 1975
- Theoretical calculations on an acetic acid, 5-methylimidazole, methanol hydrogen bond network: A model charge relay systemJournal of Theoretical Biology, 1974
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969