High resolution nuclear magnetic resonance studies of the active site of chymotrypsin: I. The hydrogen bonded protons of the “charge relay” system
- 5 July 1974
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 86 (3), 519-540
- https://doi.org/10.1016/0022-2836(74)90178-8
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteasesBiochemistry, 1973
- Assignment of an exchangeable low-field nitrogen-hydrogen proton resonance of ribonuclease A to the active-site hisitidine-119Biochemistry, 1973
- Conformational equilibria in α- and δ-chymotrypsin: The energetics and importance of the salt bridgeJournal of Molecular Biology, 1972
- Studies of the histidine residues of carbonic anhydrases using high-field proton magnetic resonanceBiochemistry, 1972
- High resolution nuclear magnetic resonance study of base pairing in four purified transfer RNA moleculesJournal of Molecular Biology, 1971
- Studies of the activity of chymotrypsinPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- [1] Principles of active site titration of proteolytic enzymesPublished by Elsevier ,1970
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969
- Proton Transfer, Acid‐Base Catalysis, and Enzymatic Hydrolysis. Part I: ELEMENTARY PROCESSESAngewandte Chemie International Edition in English, 1964
- FAST REACTIONS OF IMIDAZOLE STUDIED WITH RELAXATION SPECTROMETRYJournal of the American Chemical Society, 1960