Article
X-ray crystallographic studies of RNase A variants engineered at the most destabilizing positions of the main hydrophobic core: further insight into protein stability.
Proteins - 15 Nov 2009
Kurpiewska Katarzyna, Font Josep, Ribó Marc, Vilanova Maria, Lewiński Krzysztof
Abstract excerpt
To investigate the structural origin of decreased pressure and temperature stability, the crystal structure of bovine pancreatic ribonuclease A variants V47A, V54A, V57A, I81A, I106A, and V108A was solved at 1.4-2.0 A resolution and compared with the structure of wild-type protein. The introduced mutations had only minor influence on the global structure of ribonuclease A. The structural changes had individual...
Topics
- Animals
- Cattle
- Crystallography, X-Ray
- Escherichia coli
- Models, Molecular
- Mutagenesis
- Mutagenesis, Site-Directed
- Mutation
- Pancreas
- Protein Folding
- Protein Structure, Secondary