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  2. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    At the regulatory site, the binding of a ligand may elicit amplified or inhibited protein function. [ 4 ] [ 22 ] The binding of a ligand to an allosteric site of a multimeric enzyme often induces positive cooperativity, that is the binding of one substrate induces a favorable conformation change and increases the enzyme's likelihood to bind to ...

  3. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    If several ligand binding sites exist, but ligand binding to any one site does not affect the others, the receptor is said to be non-cooperative. Cooperativity can be homotropic , if a ligand influences the binding of ligands of the same kind, or heterotropic , if it influences binding of other kinds of ligands.

  4. Molecular binding - Wikipedia

    en.wikipedia.org/wiki/Molecular_binding

    Molecular binding occurs in biological complexes (e.g., between pairs or sets of proteins, or between a protein and a small molecule ligand it binds) and also in abiologic chemical systems, e.g. as in cases of coordination polymers and coordination networks such as metal-organic frameworks.

  5. Avidity - Wikipedia

    en.wikipedia.org/wiki/Avidity

    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 plus their orientation and immobilization. [citation needed]

  6. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is apparently increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding ...

  7. Ligand (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Ligand_(biochemistry)

    In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein.

  8. Ligand - Wikipedia

    en.wikipedia.org/wiki/Ligand

    A ligand exchange (also called ligand substitution) is a chemical reaction in which a ligand in a compound is replaced by another. Two general mechanisms are recognized: associative substitution or by dissociative substitution .

  9. 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]