Cooperativity is a phenomenon displayed by systems involving identical or near-identical elements, which act non-independently of each other, relative to a hypothetical standard non-interacting system in which the individual elements are acting independently. One manifestation of this are enzymes or receptors that have multiple binding sites where...
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in enzymology, a phenomenon in which the shape of one subunit of an enzyme consisting of several subunits is altered by the substrate (the substance ... [1 related articles]
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http://www.britannica.com/eb/a-z/c/138
Cooperativity is the interaction process by which binding of a ligand to one site on a macromolecule (enzyme, receptor, etc.) influences binding at a second site, e.g. between the substrate binding sites of an allosteric enzyme. Cooperative enzymes typically display a sigmoid (S-shaped) plot of the reaction rate against substrate concentration. (S...
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http://www.chem.qmul.ac.uk/iupac/medchem/ah.html
Cooperativity is the interaction process by which binding of a ligand to one site on a macromolecule (enzyme, receptor, etc.) influences binding at a second site, e.g. between the substrate binding sites of an allosteric enzyme. Cooperative enzymes typically display a sigmoid (S-shaped) plot of the reaction rate against substrate concentration. (Se...
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http://www.chemistry-dictionary.com/definition/cooperativity.php
Phenomenon displayed by enzymes or receptors that have multiple binding sites. Binding of one ligand alters the affinity of the other site. Both positive and negative cooperativity are known, positive cooperativity gives rise to a sigmoidal binding curve. Cooperativity is often invoked to account for nonlinearity of binding data, although it is by ...
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Phenomenon displayed by enzymes or receptors that have multiple binding sites. Binding of one ligand alters the affinity of the other site(s). Both positive and negative cooperativity are known; positive cooperativity gives rise to a sigmoidal binding curve. Cooperativity is often invoked to account for non-linearity of binding data, although it is by no means the only possible cause.
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Type: Term Pronunciation: kō-op′er-ă-tiv′i-tē Definitions: 1. A property of certain proteins (often enzymes) in which the binding curves or saturation curves or, in the case of enzymes, a plot of initial rates as a function of initial substrate concentration, are nonhyperbolic; suggests that the binding of a ligand has a ...
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http://www.medilexicon.com/medicaldictionary.php?t=20250
the increase or decrease in the rate of interaction between a reactant and a protein as the reactant concentration increases.
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