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Cooperativity is a phenomenon displayed by systems involving identical or near-identical elements, which act dependently of each other, relative to a hypothetical standard non-interacting system in which the individual elements are acting independently.
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:
The Hill coefficient, or , may describe cooperativity (or possibly other biochemical properties, depending on the context in which the Hill equation is being used). When appropriate, [clarification needed] the value of the Hill coefficient describes the cooperativity of ligand binding in the following way:
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.
An allosteric transition of a protein between R and T states, stabilised by an Agonist, an Inhibitor and a Substrate. 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.
This is a phenomenon called long-range cooperativity. Upon formation of the octamer, cI dimers may cooperatively bind to O L 3 and O R 3, repressing transcription of cI. This autonegative regulation ensures a stable minimum concentration of the repressor molecule and, should SOS signals arise, allows for more efficient prophage induction. [25]
Host guest complexation is pervasive in biochemistry. Many protein hosts recognize and hence selectively bind other biomolecules. When the protein host is an enzyme, the guests are called substrates.
In biochemistry, allosteric regulation (or allosteric control) is the regulation of a protein by binding an effector molecule at a site other than the enzyme's active site. The site to which the effector binds is termed the allosteric site.