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. 2010 Apr 21;98(8):1396–1407. doi: 10.1016/j.bpj.2009.12.4307

Figure 6.

Figure 6

Typical cases for the scaffold protein model shown in Fig. 5. (a) Plot, assuming eight phosphosites (n = 8), showing how the fraction of free B that is fully phosphorylated varies with the concentration of kinase A. The value α is the fold-change in the scaffold binding rates (i.e., α=kia/ki1a). For each value of α, the corresponding effective Hill number nH is also shown. Each curves is normalized by setting its EC50 to 1. (b) Hill coefficients as a function of number of phosphosites and fold change of scaffold binding rates with each phosphorylation. (c) Hill coefficients as a function of number of phosphosites and fold change of scaffold dissociation rates with each phosphorylation. (d) Hill coefficients as a function of number of phosphosites and simultaneous fold change of scaffold binding and dissociate rates at each phosphorylation, with λi = kia/kid = 1. (e) The same as panel c except ki/ki−1 = 2 and di/di–1 = 1/2 for all i. (f) Hill coefficients as a function of the number of phosphorylation sites and the total amount scaffold. In this case, the parameters are α = β = 4, λi = kia/kid = 1, ki/ki−1 = 2, and di/di–1 = 1/2. In panels af, St = 15, Bt = 10, with all other parameters equal to 1 except as specified otherwise in the figure.