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Table 1 Ca2+-CaM dissociation constants derived by the different mathematical models.

From: Elucidating the mechanisms of cooperative calcium-calmodulin interactions: a structural systems biology approach

Proteins Hill Adair present model Reference
PhK5 KD 1= 0.24, KD 2= 13   K1 = 1, Kc1 = 1, K2 = 1, Kc2 = 1 [33]
skMLCK KD 1= 0.02, KD 2= 0.08   K1 = 0.04, Kc1 = 0.02, K2 = 0.04, Kc2 = 0.02  
sk-N11 KD 1= 0.26, KD 2= 6   K1 = 1.2, K2 = 0.5 K1 = 5, K2 = 1  
sk-C10 KD 1= 3.4, KD 2= 4   K1 = 0.06, Kc1 = 0.02, K2 = 0.06, Kc2 = 0.02  
CaATPase KD 1= 0.09, KD 2= 0.2   K1 = 0.15, Kc1 = 0.05, K2 = 0.15, Kc2 = 0.05  
ATPase-N18 KD 1= 0.12, KD 2= 3.9   K1 = 2, Kc1 = 1, K2 = 2, Kc2 = 1  
ATPase-C17 KD 1= 0.66, KD 2= 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  
  1. 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.