Dynamic model of Escherichia coli tryptophan operon shows an optimal structural design.

A mathematical model has been developed to study the effect of external tryptophan on the trp operon. The model accounts for the effect of feedback repression by tryptophan through the Hill equation. We demonstrate that the trp operon maintains an intracellular steady-state concentration in a fivefold range irrespective of extracellular conditions. Dynamic behavior of the trp operon corresponding to varying levels of extracellular tryptophan illustrates the adaptive nature of regulation. Depending on the external tryptophan level in the medium, the transient response ranges from a rapid and underdamped to a sluggish and highly overdamped response. To test model fidelity, simulation results are compared with experimental data available in the literature. We further demonstrate the significance of the biological structure of the operon on the overall performance. Our analysis suggests that the tryptophan operon has evolved to a truly optimal design.

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