The Conformation of Substrates during Hydrolysis at the Active Site of Chymotrypsin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
1. AN INVERSION OF THE USUAL ANTIPODAL SPECIFICITY OBSERVED IN α-CHYMOTRYPSIN CATALYZED REACTIONS1
2. AN EXPLANATION OF AN ANOMALOUS ANTIPODAL SPECIFICITY OF CHYMOTRYPSIN
3. An Interpretation of the Apparent Inversion of Antipodal Specificity of α-Chymotrypsin
4. Steric Course and Specificity of α-Chymotrypsin-catalyzed Reactions. I
5. Steric Course and Specificity of α-Chymotrypsin-catalyzed Reactions. II
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1. Probing the Active Sites of Enzymes with Conformationally Restricted Substrate Analogs;Progress in Physical Organic Chemistry;2007-04-04
2. Chemoselectivity of chemically modified α-chymotrypsin;Tetrahedron;1995-02
3. A proposal for a three-dimensional representation of the S1 subsite of α-chymotrypsin;Bioorganic & Medicinal Chemistry Letters;1993-06
4. Enantiomeric specificity at the deacylation process of tryptic catalysis;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1987-11
5. On the photoreactivity of benzodihydrofurans and 2,4-cyclohexadien-1-ones;Tetrahedron Letters;1982-01
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