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  2. Hill equation (biochemistry) - Wikipedia

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

    The Hill equation reflects the occupancy of macromolecules: the fraction that is saturated or bound by the ligand. [1] [2] [nb 1] This equation is formally equivalent to the Langmuir isotherm. [3] Conversely, the Hill equation proper reflects the cellular or tissue response to the ligand: the physiological output of the system, such as muscle ...

  3. 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 ...

  4. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:

  5. 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.

  6. Ligand (biochemistry) - Wikipedia

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

    In DNA-ligand binding studies, the ligand can be a small molecule, ion, [1] or protein [2] which binds to the DNA double helix. The relationship between ligand and binding partner is a function of charge, hydrophobicity, and molecular structure. Binding occurs by intermolecular forces, such as ionic bonds, hydrogen bonds and Van der Waals forces.

  7. 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 → ...

  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. A generalized example of ligand association

  9. 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.