Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity.

@article{ONeil1987FluorescencePO,
  title={Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity.},
  author={Karyn T O'Neil and Henry R Wolfe and Susan K Erickson-Viitanen and William F. DeGrado},
  journal={Science},
  year={1987},
  volume={236 4807},
  pages={1454-6}
}
A basic amphiphilic alpha-helix is a structural feature common to many calmodulin-binding peptides and proteins. A set of fluorescent analogues of a very tight binding inhibitor (dissociation constant of 200 picomolar) of calmodulin has been synthesized. The fluorescent amino acid tryptophan has been systematically moved throughout the sequence of this peptide. The fluorescence properties for the peptides repeat every three to four residues and are consistent with the periodicity observed for… CONTINUE READING