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  2. Hill equation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Hill_equation_(biochemistry)

    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:

  3. 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:

  4. Cooperativity - Wikipedia

    en.wikipedia.org/wiki/Cooperativity

    One manifestation of this is enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is apparently increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example, when an oxygen atom binds to one of hemoglobin's four binding ...

  5. Monod–Wyman–Changeux model - Wikipedia

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

    This model explains sigmoidal binding properties (i.e. positive cooperativity) as change in concentration of ligand over a small range will lead to a large increase in the proportion of molecules in the R state, and thus will lead to a high association of the ligand to the protein. It cannot explain negative cooperativity.

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Negative cooperativity occurs when binding of the first substrate decreases the affinity of the enzyme for other substrate molecules. Allosteric enzymes include mammalian tyrosyl tRNA-synthetase, which shows negative cooperativity, [37] and bacterial aspartate transcarbamoylase [38] and phosphofructokinase, [39] which show positive cooperativity.

  7. 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.

  8. Reversible Hill equation - Wikipedia

    en.wikipedia.org/wiki/Reversible_Hill_Equation

    Hofmeyr and Cornish-Bowden first published the reversible form of the Hill equation. [1] The equation has since been discussed elsewhere [ 3 ] [ 4 ] and the model has also been used in a number of kinetic models such as a model of Phosphofructokinase and Glycolytic Oscillations in the Pancreatic β-cells [ 5 ] or a model of a glucose-xylose co ...

  9. Ultrasensitivity - Wikipedia

    en.wikipedia.org/wiki/Ultrasensitivity

    where is the Hill coefficient which quantifies the steepness of the sigmoidal stimulus-response curve and it is therefore a sensitivity parameter. It is often used to assess the cooperativity of a system. A Hill coefficient greater than one is indicative of positive cooperativity and thus, the system exhibits ultrasensitivity. [34]