Article
Comparison of metal ion-induced conformational changes in parvalbumin and oncomodulin as probed by the intrinsic fluorescence of tryptophan 102.
The Journal of biological chemistry - 15 Jul 1990
Hutnik C M, MacManus J P, Banville D, Szabo A G
Abstract excerpt
The calcium-induced conformational changes of the 108-amino acid residue proteins, cod III parvalbumin and oncomodulin, were compared using tryptophan as a sensitive spectroscopic probe. As native oncomodulin is devoid of tryptophan, site-specific mutagenesis was performed to create a mutant prot...
Topics
- Amino Acid Sequence
- Animals
- Apoproteins
- Calcium
- Calcium-Binding Proteins
- Fishes
- Magnesium
- Models, Molecular
- Molecular Sequence Data
- Muscle Proteins
- Mutation
- Neoplasm Proteins
- Parvalbumins
- Sequence Homology, Nucleic Acid
- Spectrometry, Fluorescence
- Tryptophan