Article
Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface.
Biochemistry - 14 Mar 1995
Pielak G J, Auld D S, Beasley J R, Betz S F, Cohen D S, Doyle D F, Finger S A, Fredericks Z L, Hilgen-Willis S, Saunders A J
Abstract excerpt
Random mutant libraries with substitutions at the interface between the N- and C-terminal helices of Saccharomyces cerevisiae iso-1-cytochrome c were screened. All residue combinations that have been identified in naturally occurring cytochrome c sequences are found in the libraries. Mutants with...
Topics
- Amino Acid Sequence
- Animals
- Biological Evolution
- Conserved Sequence
- Cytochrome c Group
- Genetic Variation
- Hot Temperature
- Models, Chemical
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Protein Denaturation
- Protein Structure, Secondary
- Proteins
