dissociation constant

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dissociation constant

[də‚sō·sē′ā·shən ‚kän·stənt]
(physical chemistry)
A constant whose numerical value depends on the equilibrium between the undissociated and dissociated forms of a molecule; a higher value indicates greater dissociation.
References in periodicals archive ?
4'OH-PCB 12 had the highest-affinity binding in this study, and it exhibited a significantly lower dissociation constant ([K.
We fitted corrected titration data for BL22P1B11 with a single-site binding model to determine the equilibrium dissociation constant ([K.
The four levels of the enzyme saturation with substrate S (S stands for PEP in this particular case) can be presented by the following schemes, where the substrate interaction with the first subunit is quantified by the dissociation constant K, affinity for the second substrate molecule is quantified by [alpha]K, and affinity for the third and fourth substrate molecules by [beta]K and [gamma]K, respectively [14].
Base 2 (4275 molecules, 7844 pKas) Dissociation Constants of Organic Bases in Aqueous Solution, Supplement 1972, by D.
The dissociation rates and equilibrium dissociation constants for each combinatorial mutant, determined by flow cytometry in the selection diluent, are listed in Table 2.
Conductometric, potentiometric, and spectrophotometric determination of dissociation constants of substituted benzoic acids in acetonitrile J.
Table 1: Dissociation Constants and Calculated Free Energy for Enzyme/Actin Interactions.
The calculated dissociation constant was similar to my estimated value, and the method had promise for clinical application because it directly measured the minute concentration of unbound bilirubin, which Odell's work suggested was the critical parameter for bilirubin entry into the brain.
Dan Sexton, investigator, Dyax Corporation, also spoke at the conference in a presentation entitled "A Microarray-Based Surface Plasmon Resonance Method for the Rapid Determination of Phage Display Derived Human Antibody Dissociation Constants.
However, for understanding the inhibition mechanism as well as for rational design of the protein kinase bisubstrate inhibitors, it is necessary to evaluate the effectiveness of the interaction of these compounds with the enzyme not only on the IC50 level, but also on the level of the true dissociation constants.