Article
Multisite fluorescence in proteins with multiple tryptophan residues. Apomyoglobin natural variants and site-directed mutants.
The Journal of biological chemistry - 17 Nov 2000
Tcherkasskaya O, Bychkova V E, Uversky V N, Gronenborn A M
Abstract excerpt
Time-resolved fluorescence experiments were carried out on a variety of apomyoglobins with one or two tryptophan (Trp) residues located at invariant positions 7 and 14 in the primary sequence. In all cases, the Trp fluorescence kinetics were resolved adequately into two discrete lifetime domains, and decay-associated spectra (DAS) were obtained for each decay component. The DAS resolved for unfolded proteins were...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Apoproteins
- Evolution, Molecular
- Fishes
- Fluorescence
- Horses
- Hydrogen-Ion Concentration
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation