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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...

    Binding affinity carries a huge importance in medicinal chemistry, as drugs need to bind to the protein effectively within a desired range. An exothermic binding process with a favorable enthalpy is considered a desirable characteristic for specific protein binders, as it indicates strong potential for optimization and high selectivity. [ 3 ]

  4. Methods to investigate protein–protein interactions - Wikipedia

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

    The two proteins are then mixed and the data outputs the fraction of the labeled protein that is unbound and bound to the other protein, allowing you to get a measure of K D and binding affinity. You can also take time-course measurements to characterize binding kinetics.

  5. 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]

  6. Scoring functions for docking - Wikipedia

    en.wikipedia.org/wiki/Scoring_functions_for_docking

    Binding-mode – orientation of the two binding partners relative to each other in the complex The above information yields the three-dimensional structure of the complex. Based on this structure, the scoring function can then estimate the strength of the association between the two molecules in the complex using one of the methods outlined below.

  7. Scatchard equation - Wikipedia

    en.wikipedia.org/wiki/Scatchard_equation

    The Scatchard equation is an equation used in molecular biology to calculate the affinity and number of binding sites of a receptor for a ligand. [1] It is named after the American chemist George Scatchard.

  8. Binding selectivity - Wikipedia

    en.wikipedia.org/wiki/Binding_selectivity

    Binding selectivity describes how a ligand may bind more preferentially to one receptor than another. A selectivity coefficient is the equilibrium constant for the reaction of displacement by one ligand of another ligand in a complex with the substrate. Binding selectivity is of major importance in biochemistry [1] and in chemical separation ...

  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.