Cooperativity

Cooperativity

Cooperativity is a phenomenon displayed by enzymes or receptors that have multiple binding sites where the affinity of the binding sites for a ligand is increased, positive cooperativity, or decreased, negative cooperativity, upon the binding of a ligand to a binding site. For example the affinity of hemoglobin's four binding sites for oxygen is increased above that of the unbound hemoglobin when the first oxygen molecule binds. This is referred to as cooperative binding. We also see cooperativity in large chain molecules made of many identical (or nearly identical) subunits (such as DNA, proteins, and phospholipids), when such molecules undergo phase transitions such as melting, unfolding or unwinding. This is referred to as subunit cooperativity.

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