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Single- and dual-fractal models were employed to fit the ER binding data obtained from literature.
We focus on a set of binding data obtained from 113 different protein kinases and 20 inhibitors.
Equilibrium binding data obtained from Eqs. (2) and (3) were proved to serve as stable input parameters for the generation of the competitive binding curve and the associated determination of the IC50.
However, only the models of Chen et al [17] and Hui and Bader [30] were trained on PDZ domain binding data obtained from multiple species (including human, worm and fly PDZ domains), making them thus the best choice for a multi-species analysis.
Scatchard analysis of binding data obtained from cerebellar membranes of P21 animals indicated that developmental A1254 dose-dependently increased the [H]-ryanodine binding density (Bmax) without significantly changing apparent affinities (KD).
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The association constant Ka as measured from the binding data obtained in vivo was not significantly different from the value measured in vitro when the same target DC were incubated with the 125I-Fab in test tubes.
Global fits to a single-site binding model of data obtained from at least two titrations for each site were conducted using SEDPHAT (62).
Global fits to a two-site binding model of data obtained from direct and reverse titrations of each ternary complex were conducted using SEDPHAT (62).
The data obtained from binding of type II receptor ectodomains (ECDs) as analyte to the preformed complexes were fitted by equilibrium dose response KD (eq).
In parallel comparisons from the same data obtained from the binding assays, the Scatchard plot, the Woolf plot and the saturation radioligand-binding curve gave similar estimates of the K d (7.81, 7.935 and 8.095 pL/mol, respectively) and B max (113.4, 114.5 and 115.3 pmol/L) (Table 3).
The data obtained from ligand binding to immobilized type II receptors were best fitted by equilibrium dose response KD (eq) (bold).
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