Dissociation constant

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In chemistry, biochemistry, and pharmacology, a dissociation constant 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 dissociation constant is usually denoted Kd and is the inverse of the association constant. In the special case of salts, the dissociation constant can also be called an ionization constant.

For a general reaction

in which a complex AxBy breaks down into x A subunits and y B subunits, the dissociation constant is defined

where [A], [B], and [AxBy] are the concentrations of A, B, and the complex AxBy, respectively.

Contents

Protein-ligand binding

The dissociation constant is commonly used to describe the affinity between a ligand (L) (such as a drug) and a protein (P) i.e. how tightly a ligand binds to a particular protein. Ligand-protein affinities are influenced by non-covalent intermolecular interactions between the two molecules such as hydrogen bonding, electrostatic interactions, hydrophobic and Van der Waals forces. They can also be affected by high concentrations of other macromolecules, which causes macromolecular crowding.[1][2]

The formation of a ligand-protein complex (C) can be described by a two-state process

the corresponding dissociation constant is defined

where [P], [L] and [C] represent molar concentrations of the protein, ligand and complex, respectively.

The dissociation constant has molar units (M), which correspond to the concentration of ligand [L] at which the binding site on a particular protein is half occupied, i.e. the concentration of ligand, at which the concentration of protein with ligand bound [C], equals the concentration of protein with no ligand bound [P]. The smaller the dissociation constant, the more tightly bound the ligand is, or the higher the affinity between ligand and protein. For example, a ligand with a nanomolar (nM) dissociation constant binds more tightly to a particular protein than a ligand with a micromolar (μM) dissociation constant.

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