Article
Construction and characterization of a spectral probe mutant of troponin C: application to analyses of mutants with increased Ca2+ affinity.
Biochemistry - 21 Jul 1992
Pearlstone J R, Borgford T, Chandra M, Oikawa K, Kay C M, Herzberg O, Moult J, Herklotz A, Reinach F C, Smillie L B
Abstract excerpt
A spectral probe mutant (F29W) of chicken skeletal muscle troponin C (TnC) has been prepared in which Phe-29 has been substituted by Trp. Residue 29 is at the COOH-terminal end of the A helix immediately adjacent to the Ca2+ binding loop of site I (residues 30-41) of the regulatory N domain. Since this protein is naturally devoid of Tyr and Trp, spectral features can be assigned unambiguously to the single Trp....
Topics
- Animals
- Calcium
- Calcium-Binding Proteins
- Chickens
- Circular Dichroism
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding
- Protein Conformation
