ABSTRACT
In order to characterize the binding between a ligand and a receptor, three properties are of particular interest: the equilibrium binding constant K describes the ratio between bound and unbound ligands for a given concentration of receptor under steady-state conditions. The two reaction rate constants ka and kd determine the association rate of complex formation and the dissociation rate of its disintegration respectively. Knowing two of the three parameters K, ka and kd allows the determination of the third one via K ka/kd. The knowledge of K gives a very global range of information on the binding behaviour at equilibrium conditions, the knowledge of ka and kd can reveal some details about molecular mechanism (see for example Cantor and Schimmel 1980).
