Article
Effects of amino acid replacements on the reductive unfolding kinetics of pancreatic trypsin inhibitor.
Biochemistry - 8 Feb 1994
Mendoza J A, Jarstfer M B, Goldenberg D P
Abstract excerpt
In order to characterize the major transition states in the disulfide-coupled folding pathway of bovine pancreatic trypsin inhibitor (BPTI), the reductive unfolding kinetics of wild-type BPTI and 18 variants with single amino acid replacements were measured in the presence of varying concentrations of dithiothreitol (DTTSHSH). As observed previously for the wild-type protein, unfolding of the mutant proteins was...
Topics
- Amino Acids
- Aprotinin
- Kinetics
- Mutation
- Protein Conformation
- Protein Folding
- Recombinant Proteins