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In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.
The build-up of analyte over time allows to quantify on rates (kon), off rates (koff), dissociation constants (Kd) and, in some applications, active concentrations of the analyte. [14] Several different vendors offer SPR-based devices. Best known are Biacore instruments which were the first commercially available.
The Hill equation is used extensively in pharmacology to quantify the functional parameters of a drug [citation needed] and are also used in other areas of biochemistry. The Hill equation can be used to describe dose-response relationships, for example ion channel open-probability (P-open) vs. ligand concentration.
Unless the complex is very long lived under gel conditions, or dissociation during electrophoresis is taken into account, the number derived is an apparent Kd. If the protein concentration is not known but the complex stoichiometry is, the protein concentration can be determined by increasing the concentration of DNA probe until further ...
The distribution constant (or partition ratio) (K D) is the equilibrium constant for the distribution of an analyte in two immiscible solvents. [1] [2] [3]In chromatography, for a particular solvent, it is equal to the ratio of its molar concentration in the stationary phase to its molar concentration in the mobile phase, also approximating the ratio of the solubility of the solvent in each phase.
The dissociation rate in chemistry, biochemistry, and pharmacology is the rate or speed at which a ligand dissociates from a protein, for instance, a receptor. [1] It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor. [1]
A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]
The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: