Article
Diverse interactions between the individual mutations in a double mutant at the active site of staphylococcal nuclease.
Biochemistry - 18 Sept 1990
Weber D J, Serpersu E H, Shortle D, Mildvan A S
Abstract excerpt
In principle, the quantitative effect of a second mutation on a mutant enzyme may be antagonistic, absent, partially additive, additive, or synergistic with respect to the first mutation. Depending on the kinetic or thermodynamic parameter measured, the D21E and R87G mutations of staphylococcal n...
Topics
- Binding Sites
- Calcium
- DNA
- Kinetics
- Manganese
- Micrococcal Nuclease
- Models, Molecular
- Mutation
- Protein Conformation
- RNA
- Recombinant Fusion Proteins
- Thermodynamics