Journal of Biophysics / 2011 / Article / Fig 6

Research Article

EI of the Phosphotransferase System of Escherichia coli: Mathematical Modeling Approach to Analysis of Its Kinetic Properties

Figure 6

Fitted experimental data on phosphorylation of the both EI and HPr. (a) experimental data from [18]: time dependences of the concentration of the phosphorylated protein (HPrP + EIP): 𝑇 = 3 7 C, pH = 7.4. Initial concentrations of components: PEP, 160 μM, HPr, 24.4 μM, EI (Nonphosphorylated monomers), (■) 157 nM, (●) 312.5 nM, (▲) 729 nM, (♦) 1.57 μM; (b),(c) Experimental data from [6]: time dependences of the concentrations of the phosphorylated EI and HPr; 𝑇 = 2 5 C, pH = 6.5, Initial concentrations of the components: (b) EI (Nonphosphorylated monomers): 140 nM, PEP: 44 mkM, HPr (when present): 1.85 mkM; designations of data points: (●) phospho-EI in the absence of the HPr, (■) phospho-EI in presence of the HPr; (c) initial concentrations: EI (Nonphosphorylated monomers): 32.8 nM, PEP, 390 nM, HPr (when present): 66 nM HPr, (●) phospho-EI in the absence of the HPr, (■) phospho-EI in presence of the HPr, (▲) HPrP. (d) Experimental data from [5]: dependence of the initial HPr phosphorylation rate on the HPr concentration; 𝑇 = 2 5 C, pH = 7.2, EI (total), 1.3 μM, PEP concentrations (mM): (■)—2, (●)—0.215, (▲)—0.115, (♦)—0.0615.
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579402.fig.006b
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579402.fig.006c
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