Figure 7.

Ca²⁺-dependent interaction of CaM with target protein peptides. The data from [33] shows Ca²⁺ binding to CaM in the presence of peptides derived from phosphorylase kinase (PhK5), erythrocyte Ca²⁺ CaATPase, skeletal Myosin Light Chain Kinase (skMLCK) (A). (B) and (C) show the Ca²⁺ binding to CaM in the presence of parts of skMLCK and CaATPase peptides, respectively [33]. Interaction data for Ca²⁺-CaM complexes in the presence and absence of protein kinase II (CaMPKII) reveal parameters of complex formation reaction [49]. The solid line in each case shows the model prediction for Ca²⁺-CaM binding. K₁ is macroscopic Ca²⁺ dissociation constant, Kc₁ is the cooperatively affected dissociation constants. Arrows indicate the number of Ca²⁺ ions bound to CaM required to create a complex with a target molecule peptide.