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The mean and standard error of the mean of binding constants and corresponding thermodynamics of binding are reported.
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Since ITC provides more binding characteristics than fluorescence, we used it to determine the Ca2+ binding constants and the corresponding thermodynamic parameters.
K t is the equilibrium binding constant and corresponds to the maximum binding energy, and B is the constant related to the heat of adsorption.
The binding constants and binding capacity were calculated, and the nature of binding was found to be noncovalent.
Using flow dialysis, Banfi et al. determined the macroscopic (stoichiometric) binding constants and derived their intrinsic binding constants (Ka) for the binding of the 1st - 4th Ca2+ ions to CaBD assuming independent binding among Ca2+ binding sites [6].
The quenching rate constants, binding constants, and number of binding sites were calculated in the presence of CSB.
Correlations between the binding constants and the predicted binding scores when using only low-energy conformers as docking input.
Because binding takes place in a constant flow environment, the technique can be used to extract binding constants and affinities.
These are a collection of biochemical assays measuring binding constants and enzyme inhibition values.
The obtained quenching mechanisms, binding constants, binding sites and corresponding thermodynamic parameters at different temperatures indicate that the hydrophobic interaction play a major role in the morin-BSA association.
The binding constant is the product of a charge-independent quantity, the intrinsic binding constant, and a cooperativity function.
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