Cooperative binding
In
biochemistry, a
macromolecule has
cooperative binding if when binding a
ligand, the affinity of the ligand for the molecule
changes depending on the amount of ligand already bound. A macromolecule is said to have
positive cooperativity if the binding of ligand increases affinity for the ligand, and
negative cooperativity if the affinity for the ligand decreases as more ligand is bound. A macromolecule is
noncooperative if the amount of ligand bound does not affect the binding affinity at all. In this last case, the way the affinity depends on the
concentration of ligand in solution often is described as "hyperbolic," because a graph of this dependence traces a
hyperbola). Cooperative binding is often described as "sigmoid," after the subtle "S"-shape of the graphs.
See also: quaternary structure -- enzyme allostery