Photolabeling of calmodulin with basic, amphiphilic alpha-helical peptides containing p-benzoylphenylalanine.

@article{ONeil1989PhotolabelingOC,
  title={Photolabeling of calmodulin with basic, amphiphilic alpha-helical peptides containing p-benzoylphenylalanine.},
  author={Karyn T O'Neil and Susan K Erickson-Viitanen and William F. DeGrado},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 24},
  pages={14571-8}
}
A novel photoreactive amino acid has been incorporated synthetically into two model peptides and the calmodulin-binding domain from myosin light chain kinase. Cross-linked photoadducts of each peptide with calmodulin have been prepared and digested by chemical and/or enzymatic methods to determine the site of label attachment. Depending on the position of the photoprobe in the peptide sequence, either Met-144 or Met-71 is photolabeled. These results are discussed in relation to the three… CONTINUE READING

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