Article
Equilibrium unfolding of yeast phosphoglycerate kinase and its mutants lacking one or both native tryptophans: a circular dichroism and steady-state and time-resolved fluorescence study.
Biochemistry - 1 Mar 1994
Szpikowska B K, Beechem J M, Sherman M A, Mas M T
Abstract excerpt
Yeast 3-phosphoglycerate kinase contains two tryptophans, both situated in the carboxy-terminal domain, and seven tyrosines, five in the amino-terminal domain, one in the domain-domain interface, and one in the carboxy-terminal domain. Site-specific mutagenesis has been used to construct two sing...
Topics
- Circular Dichroism
- Mutation
- Phosphoglycerate Kinase
- Protein Conformation
- Protein Folding
- Saccharomyces cerevisiae
- Spectrometry, Fluorescence
- Spectrophotometry, Ultraviolet
- Tryptophan