Quantitative interpretations of double mutations of enzymes.

Abstract excerpt

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 which kinetic or thermodynamic parameter of an enzyme is measured, the same two mutations can interact differently in the double mutant. Additive effects of two mutations on an equilibrium constant, such as the dissociation...

Topics

• Amino Acid Sequence
• Enzymes
• Glutathione Reductase
• Kinetics
• Mathematics
• Micrococcal Nuclease
• Models, Molecular
• Models, Theoretical
• Mutation
• Protein Conformation
• Steroid Isomerases