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The FRET data were fit with the two-component titration equation described previously (39).
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These values in combination with titration equations provide the necessary volumes of water, ink and Intralipid to achieve desired phantom optical properties [ 57].
Therefore, the titration curve equation applied in the non-linear curve fitting function procedure was Eq. 2.
A titration formula like Equation 1 puts the control algorithm in the class of the so-called PID controllers.
For the binding of Rox-DprC to mC1, KD is 3.8 ± 0.5 μM the value was obtained by fitting the titration data with the equation: ΔmP = ΔmPmax × [P]/([P] + KD), where ΔmP is the polarization change of Rox-DprC, [P] is the concentration of protein, and both KD and ΔmPmax are the fitting variables.
However, the Hill equation fits of the titration curves are satisfactory only to a CBZ concentration of ca. 700 μM; at higher concentrations, there is evident systematic deviation of the experimental data from the equation curve.
The redox titration data were fitted to the Nernst equation with n = 1 using KaleidaGraph (Synergy Software co).
Good linear correlations between F0/F0 − F and 1/[M] were observed (indicated by R2 values in Table 2) and the titration data were fitted to the modified Stern Volmer equation to calculate LogK and %f.
The fit of the titration kinetics was performed using a dose response function (Equation 2) (a, ECmax; b, EC50; c, ECbaseline).
The redox-titration data (signal amplitude vs set potential) were fit using the Nernst equation or evaluated qualitatively for the midpoint potential of the titration, but only limited low potential data were available or included in the fitting, and the stoichiometries of the reduced clusters were not measured (only assumed).
1A titration curve was fitted with a linear free energy equation to calculate the transition point of unfolding.
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