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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:
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.
Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other. It is formed when atoms or molecules bind together by sharing of electrons. It often, but not always, involves some chemical bonding.
The brackets around chemical species denote their concentrations. [] + [] [] One measure of how well a molecule fits a receptor is its binding affinity, which is inversely related to the dissociation constant K d. A good fit corresponds with high affinity and low K d.
Cooperative binding occurs in a molecular binding system where two or more ligand molecules can bind to a receptor molecule. Binding can be considered "cooperative" if the actual binding of the first molecule of the ligand to the receptor changes the binding affinity of the second ligand molecule.
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 ...
Binding selectivity describes how a ligand may bind more preferentially to one receptor than another. A selectivity coefficient is the equilibrium constant for the reaction of displacement by one ligand of another ligand in a complex with the substrate. Binding selectivity is of major importance in biochemistry [1] and in chemical separation ...
The Scatchard equation is an equation used in molecular biology to calculate the affinity and number of binding sites of a receptor for a ligand. [1] It is named after the American chemist George Scatchard.