Cooperative binding is the principle in enzyme kinetics that, in a multi-site protein, occupancy of one substrate binding site alters the protein's affinity for substrate at the remaining sites, so that fractional saturation is not a simple function of the independent statistical availability of free sites. Binding is classified as positively cooperative when prior binding raises affinity for subsequent substrate (yielding a sigmoidal saturation curve), negatively cooperative when prior binding lowers affinity beyond the statistically expected decline, and non-cooperative when affinity is unchanged (yielding the hyperbolic Michaelis–Menten-type curve). The concept belongs to enzyme kinetics and protein biochemistry, extending the two-step binding-then-catalysis model that underlies the Michaelis–Menten treatment to allosteric, multi-subunit proteins.
Cooperative binding is the principle in enzyme kinetics that, in a multi-site protein, occupancy of one substrate binding site alters the protein's affinity for substrate at the remaining sites, so t…