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==Overview==
This model for [[allosteric regulation]] of [[enzyme]]s suggests that the [[Protein subunit|subunits]] of multimeric proteins have two conformational states.<ref name=":3" /> The binding of the ligand causes conformational change in the other subunits of the multimeric protein. Although the subunits go through conformational changes independently (as opposed to in the [[MWC model]]), the switch of one subunit makes the other subunits more likely to change, by reducing the energy needed for subsequent subunits to undergo the same conformational change. In elaboration, the binding of a ligand to one subunit changes the protein's shape, thereby making it more [[Thermodynamic free energy|thermodynamically favorable]] for the other subunits to switch conformation to the high affinity state. Ligand binding may also result in negative cooperativity, or a reduced affinity for the ligand at the next binding site, a feature that makes the KNF model distinct from the MWC model, which suggests only positive cooperativity.<ref name=":0">{{Cite journal|last1=Koshland|first1=Daniel E.|last2=Hamadani|first2=Kambiz|date=2002-12-06|title=Proteomics and Models for Enzyme Cooperativity|journal=Journal of Biological Chemistry|language=en|volume=277|issue=49|pages=46841–46844|doi=10.1074/jbc.R200014200|issn=0021-9258|pmid=12189158|doi-access=free}}</ref><ref name=":5">{{Cite journal|last1=Henis|first1=Y I|last2=Levitzki|first2=A|date=1980-09-01|title=Mechanism of negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase deduced from ligand competition experiments.|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=77|issue=9|pages=5055–5059|issn=0027-8424|pmc=349994|pmid=6933545|doi=10.1073/pnas.77.9.5055|bibcode=1980PNAS...77.5055H|doi-access=free}}</ref> It is named KNF after [[Daniel E. Koshland Jr.|Koshland]], Némethy and Filmer, who first suggested the model
== History ==
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