a thesis in the record
Nuclear Magnetic Resonance Studies of the Catalytic Mechanism of Proteolytic Enzymes: I. Ionization Behavior of the Histidine Residue in the Catalytic Triad Of α-Lytic Protease : Implications for the Catalytic Mechanism of Serine Proteases. II. Ionization Behavior of Enzymic and Inhibitor Groups in the Tetrahedral Adduct Between α -Lytic Protease and a Peptide Aldehyde. III. Kinetics Of Pepsin-Catalyzed Hydrolysis Of N-Tri-Fluoroacetyl Amino Acids
1974 · California Institute of Technology · doctoral · Chemistry
Author
Supervisor
File and licence
Cite this page
The record changes as sources are read again, so a citation says when the page was read.
bibtex
@misc{academicancestry_caltechthesis_caltechthesis_4434,
author = {{Academic Ancestry}},
title = {{Nuclear Magnetic Resonance Studies of the Catalytic Mechanism of Proteolytic Enzymes: I. Ionization Behavior of the Histidine Residue in the Catalytic Triad Of α-Lytic Protease : Implications for the Catalytic Mechanism of Serine Proteases. II. Ionization Behavior of Enzymic and Inhibitor Groups in the Tetrahedral Adduct Between α -Lytic Protease and a Peptide Aldehyde. III. Kinetics Of Pepsin-Catalyzed Hydrolysis Of N-Tri-Fluoroacetyl Amino Acids: record of a thesis}},
year = {2026},
url = {https://academicancestry.org/thesis/caltechthesis/caltechthesis%3A4434},
note = {read on 2026-10-22}
}apa
Academic Ancestry. (2026, October 22). Nuclear Magnetic Resonance Studies of the Catalytic Mechanism of Proteolytic Enzymes: I. Ionization Behavior of the Histidine Residue in the Catalytic Triad Of α-Lytic Protease : Implications for the Catalytic Mechanism of Serine Proteases. II. Ionization Behavior of Enzymic and Inhibitor Groups in the Tetrahedral Adduct Between α -Lytic Protease and a Peptide Aldehyde. III. Kinetics Of Pepsin-Catalyzed Hydrolysis Of N-Tri-Fluoroacetyl Amino Acids: Record of a thesis [Read on 2026-10-22]. https://academicancestry.org/thesis/caltechthesis/caltechthesis%3A4434