Article
Structural studies of yeast iso-1 cytochrome c mutants by resonance Raman spectroscopy.
European journal of biochemistry - 1 Oct 1991
Hildebrandt P, Pielak G J, Williams R J
Abstract excerpt
The Ser82 and Phe82 variants of yeast iso-1 cytochrome c were studied by resonance Raman spectroscopy. In both oxidation states, distinct spectral changes were observed for some of those bands in the low-frequency region, which sensitively respond to conformational perturbations of the protein environment of the heme. These bands can be assigned to modes which include strong contributions of vibrations largely...
Topics
- Crystallization
- Cytochrome c Group
- Drug Stability
- Electrochemistry
- Heme
- Hot Temperature
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Saccharomyces cerevisiae
- Spectrum Analysis, Raman
