Receptor kinetics

In biochemistry, receptor–ligand kinetics is a branch of chemical kinetics in which the kinetic species are defined by different non-covalent bindings and/or conformations of the molecules involved, which are denoted as receptor(s) and ligand(s). Receptor–ligand binding kinetics also involves the on- and off-rates of binding.

A main goal of receptor–ligand kinetics is to determine the concentrations of the various kinetic species (i.e., the states of the receptor and ligand) at all times, from a given set of initial concentrations and a given set of rate constants. In a few cases, an analytical solution of the rate equations may be determined, but this is relatively rare. However, most rate equations can be integrated numerically, or approximately, using the steady-state approximation. A less ambitious goal is to determine the final equilibrium concentrations of the kinetic species, which is adequate for the interpretation of equilibrium binding data.

A converse goal of receptor–ligand kinetics is to estimate the rate constants and/or dissociation constants of the receptors and ligands from experimental kinetic or equilibrium data. The total concentrations of receptor and ligands are sometimes varied systematically to estimate these constants.

The binding constant is a special case of the equilibrium constant ${\displaystyle K}$. It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as:

The reaction is characterized by the on-rate constant ${\displaystyle k_{\rm {on}}}$ and the off-rate constant ${\displaystyle k_{\rm {off}}}$, which have units of 1/(concentration time) and 1/time, respectively. In equilibrium, the forward binding transition ${\displaystyle {\ce {{R}+ {L}-> {RL}}}}$ should be balanced by the backward unbinding transition ${\displaystyle {\ce {{RL}-> {R}+ {L}}}}$. That is,

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