Article
Investigation of the structural basis for thermostability of DNA-binding protein HU from Bacillus stearothermophilus.
The Journal of biological chemistry - 7 Aug 1998
Kawamura S, Abe Y, Ueda T, Masumoto K, Imoto T, Yamasaki N, Kimura M
Abstract excerpt
Site-directed mutagenesis was used to identify amino acid residues essential for the thermostability of the DNA-binding protein HU from the thermophile Bacillus stearothermophilus (BstHU). Two mutants, BstHU-A27S and BstHU-V42I, in which Ala27 and Val42 in BstHU were replaced by the corresponding...
Topics
- Bacterial Proteins
- Calorimetry, Differential Scanning
- Circular Dichroism
- DNA-Binding Proteins
- Dimerization
- Endopeptidases
- Enzyme Stability
- Geobacillus stearothermophilus
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Protein Denaturation
- Protein Folding
- Protein Structure, Tertiary
- Temperature