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Figure 5 | BMC Systems Biology

Figure 5

From: Thermodynamic modeling of transcription: sensitivity analysis differentiates biological mechanism from mathematical model-induced effects

Figure 5

Sensitivity analysis using the HDMR global sensitivity method on the thermodynamic model of Zinzen et al. First-, second- and the sum of first- and second-order sensitivity indices (scaled from 0.0 to 1.0), are shown. Despite the focus in the Zinzen et al. study on Dorsal-Twist cooperativity, these parameters are relatively insensitive compared to protein scaling factors. Results from representative enhancer structures: A) set 1 and B) set 2. The model parameters are shown on the horizontal axis. D, T, and S correspond to scaling factors for Dorsal, Twist, and Snail binding sites, respectively. DTr, TTr, and SSr correspond to cooperativity parameters representing Dorsal-Twist, Twist-Twist, and Snail-Snail cooperativities respectively, for the rho-like enhancer. Similarly, DTv, TTv, and SSv correspond to cooperativity parameters representing Dorsal-Twist, Twist-Twist, and Snail-Snail cooperativities respectively, for the vnd-like enhancer.

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