[koh-op-er-uh-tiv-i-tee] 
| the increase or decrease in the rate of interaction between a reactant and a protein as the reactant concentration increases. |
cooperativity
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 upon which an enzyme acts to form a product) or some other molecule so as to change the shape of a neighbouring subunit. The result is that the binding of a second substrate molecule to the second subunit of the enzyme differs in strength or velocity from that of the first, the third from the second, and so on. If the change in shape of the first subunit makes easier the binding of substrate to the second subunit, the effect is called positive cooperativity. In negative cooperativity, the binding of a molecule to the first subunit makes more difficult the binding of substrate to the second. See also allosteric control.
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