A method for zooming of nonlinear models of biochemical systems

BMC Systems Biology

Table 1 Robustness of the reduced model for large deviations from the nominal parameter point are presented for the enzyme kinetics model, with a sampling frequency of 0.1 (starting from 0.1) time units.

Param./Factor	10^-2	10^-1	10⁰	10¹	10²
k ₁	0.00053/0.0082	0.0018/0.0071	0.0010/0.0059	0.019/0.18	0.19/1.8
k _-1	0.19/1.9	0.0061/0.079	0.0010/0.0059	0.0017/0.0025	0.00024/0.0028
K ₂	0.00019/0.0060	0.00082/0.0055	0.0010/0.0059	0.035/0.23	0.21/0.39
k ₃	0.0068/0.014	0.0053/0.010	0.0010/0.0059	0.0067/0.044	0.035/0.29
K _-3	0.020/0.30	0.0048/0.032	0.0010/0.0059	0.0051/0.0093	0.0069/0.015
All	0.012/1.2	0.0014/0.062	0.0010/0.0059	0.025/0.41	0.010/0.045

The nominal parameter values (k₁ = 1000, k_-1 = 2000, k₂ = 1, k₃ = 1000, and k_-3 = 3000) are modified by a multiplicative factor, and the maximal (for any state variable) time average/infinity norm of the relative difference between the original and the reduced model is presented above. Note that only concentrations larger than 10^-6 are considered in the analysis above, due to potential numerical inaccuracies.

ISSN: 1752-0509