Article
Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core.
Biochemistry - 22 Jun 1993
Ishikawa K, Nakamura H, Morikawa K, Kanaya S
Abstract excerpt
The crystal structure of Escherichia coli ribonuclease HI has a cavity near Val-74 within the protein core. In order to fill the cavity space, we constructed two mutant proteins, V74L and V74I, in which Val-74 was replaced with either Leu or Ile, respectively. The mutant proteins are stabilized,...
Topics
- Amino Acids
- Base Sequence
- Circular Dichroism
- Computer Simulation
- DNA, Single-Stranded
- Enzyme Stability
- Escherichia coli
- Hot Temperature
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Ribonuclease H