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This chemical equilibrium is also the ratio of the on-rate (k forward or k a) and off-rate (k back or k d) constants. Two antibodies can have the same affinity, but one may have both a high on- and off-rate constant, while the other may have both a low on- and off-rate constant.
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: R + L ⇌ RL
Avidity (functional affinity) is the accumulated strength of multiple affinities. [2] For example, IgM is said to have low affinity but high avidity because it has 10 weak binding sites for antigen as opposed to the 2 stronger binding sites of IgG, IgE and IgD with higher single binding affinities. [citation needed]
Low-affinity binding (high K i level) implies that a relatively high concentration of a ligand is required before the binding site is maximally occupied and the maximum physiological response to the ligand is achieved. In the example shown to the right, two different ligands bind to the same receptor binding site.
Affinity describes how well a drug can bind to a receptor. Faster or stronger binding is represented by a higher affinity, or equivalently a lower dissociation constant. The EC 50 should not be confused with the affinity constant, K d. While the former reflects the drug concentration needed for a level of tissue response, the latter reflects ...
It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor. [1] The dissociation rate for a particular substrate can be applied to enzyme kinetics, including the Michaelis-Menten model. [2] Substrate dissociation rate contributes to how large or small the enzyme velocity will be. [2]
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 affinity between protein and ligand is given by the equilibrium dissociation constant K d or the inverse of the association constant 1/K a (or binding constant 1/K b) that relates the concentrations of the complexed and uncomplexed species in solution. The dissociation constant is defined as K d = [] [] []