Article
A calorimetric study of the thermal stability of barstar and its interaction with barnase.
Biochemistry - 18 Apr 1995
Martínez J C, Filimonov V V, Mateo P L, Schreiber G, Fersht A R
Abstract excerpt
The temperature-induced unfolding of single, double, and triple mutants of barstar, the specific intracellular protein inhibitor of barnase from Bacillus amyloliquefaciens, has been studied by high-sensitivity differential scanning calorimetry. The thermal unfolding of barstar mutants, where at least one of the two cysteine residues in the molecule had been replaced by alanine, follows a two-state mechanism at...
Topics
- Bacterial Proteins
- Calorimetry, Differential Scanning
- Hydrogen-Ion Concentration
- Models, Chemical
- Mutation
- Protein Denaturation
- Ribonucleases
- Thermodynamics