Article
Enhanced thermodynamic stabilities of yeast iso-1-cytochromes c with amino acid replacements at positions 52 and 102.
The Journal of biological chemistry - 25 Jun 1991
Hickey D R, Berghuis A M, Lafond G, Jaeger J A, Cardillo T S, McLendon D, Das G, Sherman F, Brayer G D, McLendon G
Abstract excerpt
We have determined the structures and thermodynamic stabilities of the wild type Asn-52 and unusually thermostable mutant Ile-52 yeast iso-1-cytochromes c (Das, G., Hickey, D. R. McLendon, D., McLendon, G., and Sherman, F. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 496-499). Although both structure...
Topics
- Amino Acids
- Cytochrome c Group
- Isoenzymes
- Mutation
- Protein Conformation
- Protein Denaturation
- Saccharomyces cerevisiae
- Spectrum Analysis
- Thermodynamics