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It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL. The reaction is characterized by the on-rate constant k on and the off-rate constant k off, which have units of M −1 s −1 and s −1, respectively. In equilibrium, the forward binding transition R + L → ...
Mathematically, the Scatchard equation is related to Eadie-Hofstee method, which is used to infer kinetic properties from enzyme reaction data. Many modern methods for measuring binding such as surface plasmon resonance and isothermal titration calorimetry provide additional binding parameters that are globally fit by computer-based iterative ...
In coordination chemistry, a stability constant (also called formation constant or binding constant) is an equilibrium constant for the formation of a complex in solution. It is a measure of the strength of the interaction between the reagents that come together to form the complex. There are two main kinds of complex: compounds formed by the ...
In some cases, more than one A will bind with a single B. One way to determine the amount of A binding to B is by using a Job plot. In this method, the sum of the molar concentrations of the two binding partners (e.g. a protein and ligand or a metal and a ligand) is held constant, but their mole fractions are varied. An observable that is ...
The dissociation rate constant is defined using K off. [2] The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off + K cat)/ K on [definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K on and K off respectively.
K i is the inhibition constant for a drug; the concentration of competing ligand in a competition assay which would occupy 50% of the receptors if no ligand were present. [5] The Cheng-Prusoff equation produces good estimates at high agonist concentrations, but over- or under-estimates K i at low agonist concentrations. In these conditions ...
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.
The value of the equilibrium constant for the formation of a 1:1 complex, such as a host-guest species, may be calculated with a dedicated spreadsheet application, Bindfit: [4] In this case step 2 can be performed with a non-iterative procedure and the pre-programmed routine Solver can be used for step 3.