Article
Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates.
Biochemistry - 15 Jan 1991
Klemm J D, Wozniak J A, Alber T, Goldenberg D P
Abstract excerpt
The thermodynamics and kinetics of unfolding of 28 bacteriophage T4 lysozyme variants were compared by using urea gradient gel electrophoresis. The mutations studied cause a variety of sequence changes at different residues throughout the polypeptide chain and result in a wide range of thermodynamic stabilities. A striking relationship was observed between the thermodynamic and kinetic effects of the amino acid...
Topics
- Crystallography
- Kinetics
- Muramidase
- Mutation
- Protein Denaturation
- T-Phages
- Thermodynamics
- Urea