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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. Methods to investigate protein–protein interactions - Wikipedia

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

    MST provides information regarding the binding affinity, stoichiometry, competition and enthalpy of two or more interacting proteins. [31] [32] Rotating cell‑based ligand binding assay using radioactivity or fluorescence, is a recent method that measures molecular interactions in living cells in real-time.

  4. Scoring functions for docking - Wikipedia

    en.wikipedia.org/wiki/Scoring_functions_for_docking

    A candidate binding mode. Scoring The process of evaluating a particular pose by counting the number of favorable intermolecular interactions such as hydrogen bonds and hydrophobic contacts. Ranking The process of classifying which ligands are most likely to interact favorably to a particular receptor based on the predicted free-energy of binding.

  5. 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 ...

  6. 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 ...

  7. IC50 - Wikipedia

    en.wikipedia.org/wiki/IC50

    Half maximal inhibitory concentration (IC 50) is a measure of the potency of a substance in inhibiting a specific biological or biochemical function. IC 50 is a quantitative measure that indicates how much of a particular inhibitory substance (e.g. drug) is needed to inhibit, in vitro, a given biological process or biological component by 50%. [1]

  8. Ligand binding assay - Wikipedia

    en.wikipedia.org/wiki/Ligand_binding_assay

    A ligand binding assay (LBA) is an assay, or an analytic procedure, which relies on the binding of ligand molecules to receptors, antibodies or other macromolecules. [1] A detection method is used to determine the presence and amount of the ligand-receptor complexes formed, and this is usually determined electrochemically or through a fluorescence detection method. [2]

  9. 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. [2]