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Subsequently a one-site binding model was determined as the appropriate form of analysis for all binding data.
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The binding models were determined using HT-SELEX, the same method we have used previously to determine specificities of mammalian TFs.
A microscopic binding model is proposed based on the studies of -1EF+2EF and +1EF-2EF that determine their microscopic binding constants (kI and kII for EF1 and EF2) and the studies of NCaBD that determine their overall binding constants, β1 and β2.
The macroscopic cooperative constant ρ was then determined to be 0.333 (ρ = 4β2/β12), which indicates that the binding model is either two independent binding sites or two identical binding sites with a negative cooperativity.
As an example a tight binding model is discussed.
Plus, a hydroxyl-dependent chloride binding model is established to quantify the distance-associated chloride binding capacity.
The dynamic binding capacity was determined.
HER2 binding affinity was determined in saturation radioligand binding assays using SKBR-3 cells (1.3 × 106 HER2/cell).
The binding kinetics was determined by SPR.
In all experiments, nonspecific binding was determined and subtracted from total binding to obtain specific binding.
Specific binding was determined by subtracting non-specific binding density from total binding density.
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