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The KNF model (or induced fit model or sequential model) arose to address the possibility of differential binding states.<ref name=":1">{{Cite news|url=http://bio.libretexts.org/Core/Biochemistry/Binding/MODEL_BINDING_SYSTEMS#Free_Energy_and_Cooperativity|title=Model Binding Systems|date=2013-11-21|newspaper=Biology LibreTexts|access-date=2017-02-21|language=en-US}}</ref> Developed by Koshland, Némethy and Filmer in 1966, the KNF model describes cooperativity as a sequential process, where ligand binding alters the conformation, and thus the affinity, of proximal subunits of the protein, resulting in several different conformations that have varying affinities for a given ligand. This model suggests that the MWC model oversimplifies cooperativity in that it does not account for conformational changes of individual binding sites, opting instead to suggest a single, whole-protein conformational change.<ref name=":4" />
== Rules
The KNF model follows the structural theory of the induced fit model of substrate binding to an enzyme.<ref name=":1" /> A slight change in the conformation of an enzyme improves its binding affinity to the transition state of the ligand, thus catalyzing a reaction. This follows the KNF model, which models cooperativity as the changing conformation of the ligand binding site upon ligand binding to another subunit.
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