Stereochemistry of the Active Site of α-Chymotrypsin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
1. AN INVERSION OF THE USUAL ANTIPODAL SPECIFICITY OBSERVED IN α-CHYMOTRYPSIN CATALYZED REACTIONS1
2. On the Active Site of α-Chymotrypsin
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4. Stereochemistry of the Active Site of α-Chymotrypsin
5. Absolute conformation of chymotrypsin-bound substrates. Specific recognition by the enzyme of biphenyl asymmetry in a constrained substrate
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1. Binding of alkaloids into the S1 specificity pocket of α-chymotrypsin: Evidence from induced circular dichroism spectra;Organic & Biomolecular Chemistry;2011
2. Stereochemical resolution of racemates, in HPLC, using a chiral stationary phase based upon immobilized α-chymotrypsin. I. Structural chiral separations;Chromatographia;1999-06
3. On the Absolute Configuration of (+)-Indane-1-carboxylic Acid;Helvetica Chimica Acta;1982-02-03
4. On the Absolute Configuration of Indane-1-carboxylic Acid;Helvetica Chimica Acta;1982-02-03
5. Enzymatic Catalysis;Enzymes in Anesthesiology;1978
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