Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference37 articles.
1. The Determination of the Concentration of Hydrolytic Enzyme Solutions: α-Chymotrypsin, Trypsin, Papain, Elastase, Subtilisin, and Acetylcholinesterase1
2. Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.
3. The dielectric constant of the solution in the diffuse and Helmholtz double layers at a charged interface in aqueous solution
4. A sensitive new substrate for chymotrypsin
5. A comparison of crystallographic data of the subtilopeptidases B and C
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