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  2. Cooperative binding - Wikipedia

    en.wikipedia.org/wiki/Cooperative_binding

    Cooperative binding occurs in molecular binding systems containing more than one type, or species, of molecule and in which one of the partners is not mono-valent and can bind more than one molecule of the other species. In general, molecular binding is an interaction between molecules that results in a stable physical association between those ...

  3. 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 ...

  4. Hill equation (biochemistry) - Wikipedia

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

    The binding of a ligand to a macromolecule is often enhanced if there are already other ligands present on the same macromolecule (this is known as cooperative binding). The Hill equation is useful for determining the degree of cooperativity of the ligand(s) binding to the enzyme or receptor.

  5. Sequential model - Wikipedia

    en.wikipedia.org/wiki/Sequential_model

    The sequential model (also known as the KNF model) is a theory that describes cooperativity of protein subunits. [1] It postulates that a protein's conformation changes with each binding of a ligand, thus sequentially changing its affinity for the ligand at neighboring binding sites.

  6. Hemocyanin - Wikipedia

    en.wikipedia.org/wiki/Hemocyanin

    Hemoglobin, for comparison, has a Hill coefficient of usually 2.8–3.0. In these cases of cooperative binding hemocyanin was arranged in protein sub-complexes of 6 subunits (hexamer) each with one oxygen binding site; binding of oxygen on one unit in the complex would increase the affinity of the neighboring units. Each hexamer complex was ...

  7. Hemoglobin - Wikipedia

    en.wikipedia.org/wiki/Hemoglobin

    The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule, with the first molecules of oxygen bound influencing the shape of the binding sites for the next ones, in a way favorable for binding. This positive cooperative binding is achieved through steric conformational changes of the hemoglobin protein ...

  8. Cyclic nucleotide–gated ion channel - Wikipedia

    en.wikipedia.org/wiki/Cyclic_nucleotide–gated...

    In bacteria, the opening of CNG channels is the result of non-cooperative binding. [9] With differing concentrations of ligands, cooperative binding and non-cooperative binding arise to adapt to these differing environments. At low ligand concentrations, it is rare for a ligand to cooperatively bind, because cooperative binding at low ...

  9. Binding site - Wikipedia

    en.wikipedia.org/wiki/Binding_site

    In biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. [1] The binding partner of the macromolecule is often referred to as a ligand . [ 2 ]