Fragment
8.1. The Exponential
A good understanding of the binding curves is the first step in understanding the data. Let us start with the binding between two dissimilar molecules. One molecule, the analyte (A), binds to one molecule, the ligand (L) in a reversible way. The velocity or rate of binding (association) is denoted by the association rate constant ka in M-1s-1. The breaking up of the complex (dissociation) is denoted by the dissociation rate constant kd in s-1. The quotient of the kd/ka defines the equilibrium dissociation constant KD in Molar which provides the analyte concentration that will saturate 50% of the ligand. Formula (8.1) shows the rate equation for a 1 to 1 interaction between the ligand and analyte. Equation (8.2) provides the calculation of the equilibrium dissociation constant.
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