Article
Mutations in the N- and D-helices of the N-domain of troponin C affect the C-domain and regulatory function.
Biophysical journal - 1 Jan 1999
Smith L, Greenfield N J, Hitchcock-DeGregori S E
Abstract excerpt
Troponin C contains a 14-residue alpha-helix at the amino terminus, the N-helix, that calmodulin lacks. Deletion of the first 11-14 residues of troponin C alters function. In the present investigation a mutant lacking residues 1-7 of the N-helix has normal conformation, Ca2+ binding, and regulatory function. Thus, residues 8-14 of the N-helix are generally sufficient for troponin C function. In the x-ray...
Topics
- Animals
- Base Sequence
- Binding Sites
- Biophysical Phenomena
- Biophysics
- Calcium
- Chickens
- Circular Dichroism
- Cross-Linking Reagents
- In Vitro Techniques
- Mutation
- Myosins
- Oligodeoxyribonucleotides
- Protein Conformation
- Protein Structure, Secondary
- Recombinant Proteins
- Sequence Deletion
- Troponin C