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  2. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL

  3. Isothermal titration calorimetry - Wikipedia

    en.wikipedia.org/wiki/Isothermal_Titration...

    ITC is a quantitative technique that can determine the binding affinity (), reaction enthalpy (), and binding stoichiometry of the interaction between two or more molecules in solution. [15] This is achieved by measuring the enthalpies of a series of binding reactions caused by injections of a solution of one molecule to a reaction cell ...

  4. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    The method works equally well in standard buffers and biological liquids like blood or cell-lysate. It is a free solution method which does not need to immobilize the binding partners. MST provides information regarding the binding affinity, stoichiometry, competition and enthalpy of two or more interacting proteins. [31] [32]

  5. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    Affinity chromatography can be used in a number of applications, including nucleic acid purification, protein purification [9] from cell free extracts, and purification from blood. By using affinity chromatography, one can separate proteins that bind to a certain fragment from proteins that do not bind that specific fragment. [10]

  6. 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 ...

  7. Microscale thermophoresis - Wikipedia

    en.wikipedia.org/wiki/Microscale_thermophoresis

    Thermophoresis, the movement of the molecule in the temperature gradient, depends on three parameters that typically change upon interaction. Thus, the overall MST signal is plotted against the ligand concentration to obtain a dose-response curve, from which the binding affinity can be deduced.

  8. Ligand efficiency - Wikipedia

    en.wikipedia.org/wiki/Ligand_efficiency

    Ligand efficiency is a measurement of the binding energy per atom of a ligand to its binding partner, such as a receptor or enzyme. [1]Ligand efficiency is used in drug discovery research programs to assist in narrowing focus to lead compounds with optimal combinations of physicochemical properties and pharmacological properties.

  9. Filter binding assay - Wikipedia

    en.wikipedia.org/wiki/Filter_binding_assay

    In biochemistry or chemistry, filter binding assay is a simple way to quickly study many samples. One of the ways to learn about an interaction between two molecules is to determine the binding constant, which is a number that describes the ratio of unbound and bound molecules. This information reveals the affinity between the two molecules and ...