Article
The effects of hydrophilic to hydrophobic surface mutations on the denatured state of iso-1-cytochrome c: investigation of aliphatic residues.
Biochemistry - 7 Mar 1995
Herrmann L, Bowler B E, Dong A, Caughey W S
Abstract excerpt
A series of hydrophilic to hydrophobic surface mutations were prepared at the highly solvent-exposed lysine 73 of iso-1-cytochrome c to assess the ability of such mutants to affect the energetics of the denatured state. In this report, the aliphatic hydrophobics (leucine, isoleucine, valine, alanine, glycine) were studied. The thermodynamic stability of each of these mutants was determined by guanidine...
Topics
- Amino Acids
- Base Sequence
- Cytochrome c Group
- Cytochromes c
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Oligodeoxyribonucleotides
- Protein Denaturation
- Protein Structure, Secondary
- Saccharomyces cerevisiae