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Two essential assumptions guide the KNF model:<ref name=":2">{{Cite book|title=Structure and mechanism in protein science : a guide to enzyme catalysis and protein folding|last=Alan|first=Fersht|publisher=Freeman|isbn=9780716732686|oclc=837581840|year = 1999}}</ref>
# The protein exists in a single state of either low or high affinity for the ligand, when not bound to the ligand.......
# Upon ligation of a binding site, a conformational change is produced in that region of the protein. Changing this region of the protein may influence the conformation of nearby binding sites on the same protein, thus changing their affinity for the
The KNF model characterizes enzymes that exhibit what was coined by Koshland and Hamadi in 2002 as i<sup>3</sup> cooperativity.<ref name=":0" /> This term is used merely to describe the structural nature of the sequential model, as the authors provide no other proposed descriptions or types of cooperativity.<ref>{{Cite book|url=https://books.google.com/books?id=SkSQNNACcrYC&q=i3+cooperativity&pg=PA687|title=Enzyme Kinetics: Catalysis and Control: A Reference of Theory and Best-Practice Methods|last=Purich|first=Daniel L.|date=2010-06-16|publisher=Elsevier|isbn=9780123809254|language=en}}</ref> These three properties are as follows:
# the nature of the subunits of the multimeric protein are such that they are ''identical'' to each other
# ligand binding ''induces'' a conformational change in the protein
# the conformational change is an ''intramolecular'' rearrangement within the protein
The i<sup>3</sup> nature of a multimeric, cooperatively-acting protein is useful in standardizing the structural and physical basis of the sequential model.using model verification
== Comparison to the MWC model ==
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