Structure and specific binding of trypsin: Comparison of inhibited derivatives and a model for substrate binding
- 25 February 1974
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 83 (2), 209-230
- https://doi.org/10.1016/0022-2836(74)90388-x
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- The structure of bovine trypsin : Electron density maps of the inhibited enzyme at 5 Å and at 2·7 Å resolutionJournal of Molecular Biology, 1974
- The charge relay system in chymotrypsin and chymotrypsinogenJournal of Molecular Biology, 1973
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- Conformational equilibria in α- and δ-chymotrypsin: The energetics and importance of the salt bridgeJournal of Molecular Biology, 1972
- Equilibrium and rate constants for the interconversion of two conformations of α-chymotrypsin: The existence of a catalytically inactive conformation at neutral pHJournal of Molecular Biology, 1971
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1970
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1969
- The matching of physical models to three-dimensional electron-density maps: A simple optical deviceJournal of Molecular Biology, 1968
- Identification of the ionising group controlling the active conformation of δ-chymotrypsin in alkaline pHBiochemical and Biophysical Research Communications, 1967
- CRYSTALLINE TRYPSINThe Journal of general physiology, 1932