The interaction of calmodulin with the C-terminal M5 peptide of myosin light chain kinase.

The interaction with calmodulin of the 17-residue C-terminal fragment M5 of myosin light chain kinase has been studied by several physical techniques. Circular dichroism measurements suggest that M5 exists within the complex primarily as an alpha-helix. Fluorescence intensity measurements of the single tryptophan of M5 (Trp-4) indicate that it is in a relatively nonpolar environment and is shielded from solvent. Dynamic measurements of fluorescence anisotropy decay indicate that Trp-4 changes from a freely rotating fluorophore to one which is largely immobilized upon complex formation. Static fluorescence measurements show that 2,6-TNS is displaced from its binding site on calmodulin by M5. The binding of M5 also partially inhibits the proteolytic scission by trypsin of the bond between residues 77 and 78.