Table 1.

Ca²⁺-CaM dissociation constants derived by the different mathematical models.

Proteins	Hill	Adair	present model	Reference
PhK5	KD1 = 0.24, KD2 = 13		K1 = 1, Kc1 = 1, K2 = 1, Kc2 = 1	[33]
skMLCK	KD1 = 0.02, KD2 = 0.08		K1 = 0.04, Kc1 = 0.02, K2 = 0.04, Kc2 = 0.02
sk-N11	KD1 = 0.26, KD2 = 6		K1 = 1.2, K2 = 0.5 K1 = 5, K2 = 1
sk-C10	KD1 = 3.4, KD2 = 4		K1 = 0.06, Kc1 = 0.02, K2 = 0.06, Kc2 = 0.02
CaATPase	KD1 = 0.09, KD2 = 0.2		K1 = 0.15, Kc1 = 0.05, K2 = 0.15, Kc2 = 0.05
ATPase-N18	KD1 = 0.12, KD2 = 3.9		K1 = 2, Kc1 = 1, K2 = 2, Kc2 = 1
ATPase-C17	KD1 = 0.66, KD2 = 2.4		K1 = 0.4, Kc1 = 0.2 K2 = 2, Kc2 = 1
CaMKII-cbp			K1 = 0.5, Kc1 = 0.5, K2 = 0.5, Kc2 = 0.5	[49]
CaMKII			K1 = 5, Kc1 = 5, K2 = 5, Kc2 = 5
CaM pH = 7.2		K1 = 0.34, K2 = 0.36, K3 = 0.13, K4 = 0.06	K1 = 17, Kc1 = 7, K2 = 20, Kc2 = 0.5	[12]
F12		K1 = 0.142, K2 = 0.062	K1 = 17, Kc1 = 7, K2 = 17, Kc2 = 7
F34		K3 = 0.0543, K4 = 1.82	K1 = 20, Kc1 = 0.5, K2 = 20, Kc2 = 0.5
CaM pH = 6			K1 = 10, Kc1 = 5, K2 = 10, Kc2 = 5	[9]
CaM pH = 10.1			K1 = 2, Kc1 = 1.8, K2 = 2, Kc2 = 1.8

K₁ is the dissociation constant for a Ca²⁺ binding site in the N-terminal, Kc₁ is a cooperatively modified dissociation constant for a Ca²⁺ binding site in the N-terminal when a neighbouring site is occupied, K₂ is a dissociation constant for a Ca²⁺ binding site in the C-terminal, and Kc₂ is a cooperatively influenced dissociation constant for a Ca²⁺ binding site in the C-terminal when a neighbouring site is occupied. All constants shown are in μM.