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Receptor–ligand kinetics
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Receptor–ligand kinetics : ウィキペディア英語版
Receptor–ligand 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.
== Binding kinetics ==

The binding constant is a special case of the equilibrium constant K. It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as:
: + \rightleftharpoons .
The reaction is characterized by the on-rate constant k_ and the off-rate constant k_, which have units of 1/(concentration time) and 1/time, respectively. In equilibrium, the forward binding transition + \to should be balanced by the backward unbinding transition \to + . That is,
:k_\,(), (.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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