Article
Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.
Biochemistry - 26 Aug 1997
Ruvinov S, Wang L, Ruan B, Almog O, Gilliland G L, Eisenstein E, Bryan P N
Abstract excerpt
In complex with subtilisin BPN', the 77 amino acid prodomain folds into a stable compact structure comprising a four-stranded antiparallel beta-sheet and two three-turn alpha-helices. When isolated from subtilisin, the prodomain is 97% unfolded even under optimal folding conditions. Traditionally...
Topics
- Bacillus subtilis
- Calorimetry, Differential Scanning
- Circular Dichroism
- Cloning, Molecular
- Enzyme Stability
- Escherichia coli
- Hydrogen-Ion Concentration
- Kinetics
- Mutation
- Osmolar Concentration
- Protein Binding
- Protein Denaturation
- Protein Engineering
- Protein Folding
- Recombinant Proteins
- Subtilisins
- Temperature
- Thermodynamics