Article
Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk-type inhibitor of trypsin and chymotrypsin--cooperative versus autonomous refolding of subdomains.
European journal of biochemistry - 1 Feb 1998
Philipp S, Kim Y M, Dürr I, Wenzl G, Vogt M, Flecker P
Abstract excerpt
It is widely believed that protein folding is a hierarchical process proceeding from secondary structure via subdomains and domains towards the complete tertiary structure. Accordingly, protein subdomains should behave as independent folding units. However, this prediction would underestimate the...
Topics
- Amino Acid Sequence
- Base Sequence
- Chymotrypsin
- Cloning, Molecular
- DNA
- Disulfides
- Drug Stability
- Escherichia coli
- Genetic Variation
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Protein Conformation
- Protein Folding
