Dissociation constant
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.
Overview[edit | edit source]
The dissociation constant is usually denoted by Kd and is used to describe the interaction between two molecules such as a protein and a ligand. The lower the dissociation constant, the more tightly bound the ligand is, or the higher the affinity between ligand and protein.
Calculation[edit | edit source]
The dissociation constant is the inverse of the association constant (Ka) and can be calculated using the equation:
Kd = [A][B]/[AB]
where [A] and [B] are the molar concentrations of the dissociated components and [AB] is the molar concentration of the complex.
Applications[edit | edit source]
Dissociation constants are used in many areas of chemistry and biochemistry, including in the design of drugs and in the study of proteins and other macromolecules.
See also[edit | edit source]
- Chemical equilibrium
- Equilibrium constant
- Acid dissociation constant
- Base dissociation constant
- Protein-ligand binding
References[edit | edit source]
Dissociation constant Resources | ||
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Contributors: Prab R. Tumpati, MD