In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting …

Positive cooperativity implies allosteric binding – binding of the ligand at one site increases the enzyme’s affinity for another ligand at a site different from the other site. Enzymes that …

This phenomenon—currently known as the “allosteric effect”—was named the “Bohr effect” and studied as cooperative binding of ligands to distinct protein sites. Several equations, such as …

Jan 23, 2024 · “Allosteric” was first used to mean the effector that bound to “the other site” (i.e., a site distinct from the active or orthosteric site). It was used as an adjective to define a type of …

Allostery is most often associated with protein functions that respond to changes in concentrations of small molecules. However, the same principles apply when the function of a protein (or …

Inhibition and activation of enzymes via other molecules are important ways that enzymes are regulated. Inhibitors can act competitively or noncompetitively; noncompetitive inhibitors are …

Jan 21, 2025 · Most allosteric effects can be explained by the concerted MWC model put forth by Monod, Wyman, and Changeux, or by the sequential model described by Koshland, Nemethy, …

Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector (allosteric modulator) which results in an apparent change in binding affinity at a …

Allosteric effects occur when the binding properties of a macromolecule change as a consequence of a second ligand binding to the macromolecule and altering its affinity towards …

Mar 11, 2025 · One key regulatory mechanism involves allosteric sites—specific regions on an enzyme that bind regulatory molecules, altering activity without directly interacting with the …