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Photolabeling of calmodulin with basic, amphiphilic alpha-helical peptides containing p-benzoylphenylalanine
K T O'Neil1, S Erickson-Viitanen, W F DeGrado
1E. I. du Pont de Nemours & Company, Central Research and Development Department, Wilmington, Delaware 19880-0328.
Abstract:
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-dimensional structure of calmodulin obtained crystallographically and the known solution properties of calmodulin.