Cooperativity
Cooperativity
Cooperativity is a phenomenon in Biochemistry and Molecular biology that describes the increased or decreased function of an Enzyme or Protein in response to the binding of an Effector molecule at a site other than the Active site.
Pronunciation
Cooperativity: /koʊˌɑːpərəˈtɪvɪti/
Etymology
The term "Cooperativity" is derived from the English word "Cooperative", which means working together towards a common goal. In the context of biochemistry, it refers to the cooperative behavior of molecules in a system.
Definition
Cooperativity is a property of certain systems in which the shape of the system changes upon binding of one ligand, which alters the affinity of the remaining sites for ligand. This can result in a higher (positive cooperativity) or lower (negative cooperativity) affinity for subsequent ligands compared to the first.
Related Terms
- Allosteric regulation: The regulation of an enzyme or protein by binding an effector molecule at a site other than the enzyme's active site.
- Hill coefficient: A measure of the degree of cooperativity in a system.
- Hemoglobin: An example of a protein that exhibits cooperativity.
- Ligand: A substance that forms a complex with a biomolecule to serve a biological purpose.
- Enzyme kinetics: The study of the chemical reactions that are catalyzed by enzymes.
See Also
External links
- Medical encyclopedia article on Cooperativity
- Wikipedia's article - Cooperativity
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