Mutants of Bovine Pancreatic Trypsin Inhibitor Lacking Cysteines 14 and 38 Can Fold Properly
Author:
Affiliation:
1. Department of Biocatalysis, Genentech, Inc., South San Francisco, CA 94080.
2. Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference22 articles.
1. COHEN, F.E., A DIFFUSION-COLLISION-ADHESION MODEL FOR THE KINETICS OF MYOGLOBIN REFOLDING, NATURE 286: 632 (1980).
2. CREIGHTON, T.E., INTERMEDIATES IN REFOLDING OF REDUCED PANCREATIC TRYPSIN-INHIBITOR, JOURNAL OF MOLECULAR BIOLOGY 87: 579 (1974).
3. CREIGHTON, T.E., 2-DISULFIDE INTERMEDIATES AND FOLDING PATHWAY OF REDUCED PANCREATIC TRYPSIN-INHIBITOR, JOURNAL OF MOLECULAR BIOLOGY 95: 167 (1975).
4. CREIGHTON, T.E., CONFORMATIONAL RESTRICTIONS ON PATHWAY OF FOLDING AND UNFOLDING OF PANCREATIC TRYPSIN-INHIBITOR, JOURNAL OF MOLECULAR BIOLOGY 113: 275 (1977).
5. CREIGHTON, T.E., ROLE OF THE ENVIRONMENT IN THE REFOLDING OF REDUCED PANCREATIC TRYPSIN-INHIBITOR, JOURNAL OF MOLECULAR BIOLOGY 144: 521 (1980).
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