Molecular Orbital studies on the Enzymatic Reaction Mechanism of Serine Proteases. I. Charge Relay System in Substrate Free State
- 1 May 1977
- journal article
- Published by Physical Society of Japan in Journal of the Physics Society Japan
- Vol. 42 (5), 1694-1700
- https://doi.org/10.1143/jpsj.42.1694
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- The refined crystal structure of bovine β-trypsin at 1·8 Å resolution: II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7·0Journal of Molecular Biology, 1975
- Tertiary structural differences between microbial serine proteases and pancreatic serine enzymesNature, 1975
- A Family of Protein-Cutting ProteinsScientific American, 1974
- A molecular orbital study on the enzymic reaction mechanism of α-chymotrypsmJournal of Theoretical Biology, 1973
- Self-consistent-field wavefunctions for complex molecules. The approximation of partial retention of diatomic differential overlapThe Journal of Chemical Physics, 1973
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- Atomic coordinates for subtilisin BPN′ (or Novo)Biochemical and Biophysical Research Communications, 1971
- Participation of an Acidic Group in the Chymotrypsin Catalysis***The Journal of Biochemistry, 1969
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969
- The Effect of Structure on the Rates of Some α-Chymotrypsin-catalyzed ReactionsJournal of the American Chemical Society, 1962