Article
Fluorescence analysis of calmodulin mutants containing tryptophan: conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II.
Biochemistry - 30 Jul 1991
Chabbert M, Lukas T J, Watterson D M, Axelsen P H, Prendergast F G
Abstract excerpt
Peptide-induced conformational changes in five isofunctional mutants of calmodulin (CaM), each bearing a single tryptophan residue either at the seventh position of each of the four calcium-binding loops (i.e., amino acids 26, 62, 99, and 135) or in the central helix (amino acid 81) were studied...
Topics
- Amino Acid Sequence
- Animals
- Calcium
- Calmodulin
- Calmodulin-Binding Proteins
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Myosin-Light-Chain Kinase
- Protein Conformation
- Protein Kinases
- Rats
- Spectrometry, Fluorescence
- Spectrophotometry, Ultraviolet
- Tryptophan