Article
High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation.
Biochemistry - 27 Jun 1995
Akasako A, Haruki M, Oobatake M, Kanaya S
Abstract excerpt
To test whether the combination of multiple thermostabilizing mutations is a useful strategy to generate a hyperstable mutant protein, five mutations, Gly23-->Ala, His62-->Pro, Val74-->Leu, Lys95-->Gly, and Asp134-->His or Asn, were simultaneously introduced into Escherichia coli ribonuclease HI....
Topics
- Base Sequence
- Binding Sites
- Chymotrypsin
- Circular Dichroism
- Crystallization
- Endopeptidases
- Enzyme Stability
- Escherichia coli
- Hot Temperature
- Hydrogen-Ion Concentration
- Models, Molecular
- Molecular Structure
- Mutagenesis
- Mutation
- Protein Conformation
- Protein Denaturation
- Ribonuclease H
- Structure-Activity Relationship