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  2. Monod–Wyman–Changeux model - Wikipedia

    en.wikipedia.org/wiki/Monod–Wyman–Changeux_model

    In biochemistry, the Monod–Wyman–Changeux model (MWC model, also known as the symmetry model or concerted model) describes allosteric transitions of proteins made up of identical subunits. It was proposed by Jean-Pierre Changeux in his PhD thesis, and described by Jacques Monod , Jeffries Wyman , and Jean-Pierre Changeux .

  3. Allosteric enzyme - Wikipedia

    en.wikipedia.org/wiki/Allosteric_enzyme

    Two main models have been proposed to describe this mechanism: the "concerted model" of Monod, Wyman, and Changeux, [1] and the "sequential model" of Koshland, Nemethy, and Filmer. [6] In the concerted model, the protein is thought to have two “all-or-none” global states. This model is supported by positive cooperativity where binding of ...

  4. 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. It gives one explanation for cooperative binding.

  5. 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:

  6. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    Homotropic cooperativity refers to the fact that the molecule causing the cooperativity is the one that will be affected by it. Heterotropic cooperativity is where a third party substance causes the change in affinity. Homotropic or heterotropic cooperativity could be of both positives as well as negative types depend upon whether it support or ...

  7. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  8. Concerted evolution - Wikipedia

    en.wikipedia.org/wiki/Concerted_evolution

    Concerted evolution is the phenomenon where paralogous genes within one species are more closely related to one another than to members of the same gene family in closely related species. In other terms, when specific members of a family are investigated, a greater amount of similarity is found within a species rather than between species. [ 1 ]

  9. Concerted reaction - Wikipedia

    en.wikipedia.org/wiki/Concerted_reaction

    In chemistry, a concerted reaction is a chemical reaction in which all bond breaking and bond making occurs in a single step. Reactive intermediates or other unstable high energy intermediates are not involved. [1] [2] Concerted reaction rates tend not to depend on solvent polarity ruling out large buildup of charge in the transition state.

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