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  2. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    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 → ...

  3. Receptor–ligand kinetics - Wikipedia

    en.wikipedia.org/wiki/Receptor–ligand_kinetics

    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.

  4. Scatchard equation - Wikipedia

    en.wikipedia.org/wiki/Scatchard_equation

    When each receptor has a single ligand binding site, the system is described by [] + [] [] with an on-rate (k on) and off-rate (k off) related to the dissociation constant through K d =k off /k on. When the system equilibrates,

  5. Stability constants of complexes - Wikipedia

    en.wikipedia.org/wiki/Stability_constants_of...

    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 ...

  6. Avidity - Wikipedia

    en.wikipedia.org/wiki/Avidity

    The affinity constant, K a, is the inverse of the dissociation constant, K d. The strength of complex formation in solution is related to the stability constants of complexes , however in case of large biomolecules, such as receptor - ligand pairs, their interaction is also dependent on other structural and thermodynamic properties of reactants ...

  7. Dissociation rate - Wikipedia

    en.wikipedia.org/wiki/Dissociation_rate

    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.

  8. Determination of equilibrium constants - Wikipedia

    en.wikipedia.org/wiki/Determination_of...

    log 10 β values between about 2 and 11 can be measured directly by potentiometric titration using a glass electrode. This enormous range of stability constant values (ca. 100 to 10 11) is possible because of the logarithmic response of the electrode. The limitations arise because the Nernst equation breaks down at very low or very high pH.

  9. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other. It is formed when atoms or molecules bind together by sharing of electrons.