Converting Trypsin to Chymotrypsin: The Role of Surface Loops
Author:
Affiliation:
1. Hormone Research Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143- 0534.
2. Biochemistry Department, Eötvös Loránd University, Budapest, Hungary.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference44 articles.
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2. BAUER, C.A., ACTIVE-CENTERS OF STREPTOMYCES-GRISEUS PROTEASE-1, STREPTOMYCES-GRISEUS PROTEASE-3, AND ALPHA-CHYMOTRYPSIN - ENZYME-SUBSTRATE INTERACTION, BIOCHEMISTRY 17: 375 (1978).
3. BENDER, M.L., KINETICS OF ALPHA-CHYMOTRYPSIN REACTIONS IN PRESENCE OF ADDED NUCLEOPHILES, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 86: 3697 (1964).
4. BLEVINS, R.A., THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-CHYMOTRYPSIN AT 1.67-A RESOLUTION, JOURNAL OF BIOLOGICAL CHEMISTRY 260: 4264 (1985).
5. BODE, W, REFINED CRYSTAL-STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.8 A RESOLUTION .2. CRYSTALLOGRAPHIC REFINEMENT, CALCIUM-BINDING SITE, BENZAMIDINE BINDING-SITE AND ACTIVE-SITE AT PH 7.0, JOURNAL OF MOLECULAR BIOLOGY 98: 693 (1975).
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