THE ACTIVE CENTERS OF SERINE PROTEINASES
- 1 February 1974
- journal article
- review article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 227 (1) , 438-445
- https://doi.org/10.1111/j.1749-6632.1974.tb14406.x
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. Stereochemical interpretationBiochemistry, 1973
- The charge relay system in chymotrypsin and chymotrypsinogenJournal of Molecular Biology, 1973
- High resolution nuclear magnetic resonance study of the histidine—Aspartate hydrogen bond in chymotrypsin and chymotrypsinogenJournal of Molecular Biology, 1972
- Conformational equilibria in α- and δ-chymotrypsin: The energetics and importance of the salt bridgeJournal of Molecular Biology, 1972
- Mechanism of the .alpha.-chymotrypsin-catalyzed hydrolysis of amides. pH dependence of kc and km. kinetic detection of an intermediateJournal of the American Chemical Society, 1971
- Properties of the isoleucyl amino-terminus of α-chymotrypsinBiochemical and Biophysical Research Communications, 1971
- A hydrogen-bond network at the active site of subtilisin BPN'Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- Three-dimensional Structure of Tosyl-elastaseNature, 1970
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1969
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1968