The Role of Amino-Terminal Alanine in the Control of Conformation and Activity of alpha-Chymotrypsin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1982.tb07024.x/fullpdf
Reference45 articles.
1. The Correlation of the pH (pD) Dependence and the Stepwise Mechanism of α-Chymotrypsin-Catalyzed Reactions
2. Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific Substrates
3. Kinetics of α-chymotrypsin action. I. pH, solvent, and temperature effects
4. Stereochemistry of the Active Site of α-Chymotrypsin
5. Conformational states of chymotrypsin at high pH: substrate activation and sidechain interactions
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1. Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein–interface interaction: Interaction of α-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16–Asp194);Biotechnology and Bioengineering;1998-08-05
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