13C and 1H NMR Studies of Ionizations and Hydrogen Bonding in Chymotrypsin-Glyoxal Inhibitor Complexes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference42 articles.
1. 13C-NMR study of the inhibition of δ-chymotrypsin by a tripeptide-glyoxal inhibitor
2. Ionisations within a subtilisin–glyoxal inhibitor complex
3. Inhibitors of the chymotrypsin-like activity of proteasome based on di- and tri-peptidyl α-keto aldehydes (glyoxals)
4. Peptide glyoxals: a novel class of inhibitor for serine and cysteine proteinases
5. A study of the stabilization of tetrahedral adducts by trypsin and δ-chymotrypsin
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1. Kinetic Studies of the Effect of pH on the Trypsin-Catalyzed Hydrolysis of N-α-benzyloxycarbonyl-l-lysine-p-nitroanilide: Mechanism of Trypsin Catalysis;ACS Omega;2020-03-03
2. A new lysine derived glyoxal inhibitor of trypsin, its properties and utilization for studying the stabilization of tetrahedral adducts by trypsin;Biochemistry and Biophysics Reports;2016-03
3. Quantifying tetrahedral adduct formation and stabilization in the cysteine and the serine proteases;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2015-10
4. Hemiacetal stabilization in a chymotrypsin inhibitor complex and the reactivity of the hydroxyl group of the catalytic serine residue of chymotrypsin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2014-06
5. pKa determination by 1H NMR spectroscopy – An old methodology revisited;Journal of Pharmaceutical and Biomedical Analysis;2014-05
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