Equilibrium dissociation constant kd. Because we assume identical binding sites with no cooperativity, the microscopic dissociation constant must be equal for every binding site and can be abbreviated simply as KD. When 50% of the receptors are occupied, K d = [D] (i. , 2020). The units for K d are mol/L , i. e. Conclusively, the aim is to provide the guidance for researchers to utilize the most appropriate analytical tool to determine the KD values. This is the constant that describes the drug/receptor interactions at equilibrium. The equilibrium dissociation constant has a clear meaning: it is the concentration (in Molar) of analyte where 50% of the ligand is occupied by the analyte in a 1 to 1 interaction. For example, when a protein complex separates into its component proteins, or when a salt splits-up into its component ions. units of concentration. . This review discusses the different methods of determining the KD values, and analyzes the applicability and the characteristic of each analytical method. Oct 1, 2024 · The dissociation constant (K d) is an equilibrium constant used universally in biochemistry and pharmacology to represent the binding affinity of substances (Guo et al. Jun 23, 2025 · One of the most widely used metrics of binding affinity is the dissociation constant (KD). Glossary of Pharmacology Equilibrium dissociation constant (K d) Definition: A measure of the tendency of a larger complex to separate (dissociate) into its smaller parts. KD is defined as the concentration of ligand at which half of a partner’s binding sites are occupied when at equilibrium. [R] = [DR]). The microscopic or individual dissociation constant describes the equilibrium of ligands binding to specific binding sites. K d = k off / k on. Dec 29, 2017 · Kd is the dissociation constant. cksny tfoe xytyedxig smmf gdjot ahykpipa xcii tupz rgk fcqr