Figure 6.

Analysis of cooperativity in Ca2+ binding to CaM fragments and full CaM molecules. Ca2+ binding to scallop testis CaM N- and C-terminal domains (A) as well as full length CaM (D) was measured by flow dialysis in [12]. The Scatchard plots for N-terminal (B), C-terminal (C) domains, and full length CaM (E) suggest that Ca2+ binding sites are cooperatively bound in pairs within the N- and C- terminal globular domains. r is the number of mol of bound Ca2+ per mol of CaM [12]. K1 and Kc1 are the dissociation and cooperative dissociation constants for the N-terminal, while K2 and Kc2 are the dissociation and cooperative dissociation constants for the C-terminal of scallop testis CaM.

Valeyev et al. BMC Systems Biology 2008 2:48   doi:10.1186/1752-0509-2-48
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