The simulation overlays a sigmoidal allosteric velocity curve against a classic hyperbolic Michaelis-Menten curve, then lets you bind an activator or inhibitor at a regulatory site to reshape the sigmoidal curve in real time.
Use the substrate concentration slider to trace out the reaction velocity curve, and toggle the activator or inhibitor switch to see the curve shift leftward or rightward along with a change in the Hill coefficient readout.
Substrate concentration slider, kinetics mode toggle, and an activator/inhibitor selector
Hemoglobin's cooperative oxygen binding curve has a Hill coefficient of about 2.8, which is why it can load and unload oxygen so much more efficiently than non-cooperative carriers like myoglobin.
The simulation overlays a sigmoidal allosteric velocity curve against a classic hyperbolic Michaelis-Menten curve, then lets you bind an activator or inhibitor at a regulatory site to reshape the sigmoidal curve in real time.
The simulation overlays a sigmoidal allosteric velocity curve against a classic hyperbolic Michaelis-Menten curve, then lets you bind an activator or inhibitor at a regulatory site to reshape the sigmoidal curve in real time.
Use the substrate concentration slider to trace out the reaction velocity curve, and toggle the activator or inhibitor switch to see the curve shift leftward or rightward along with a change in the Hill coefficient readout.
Hemoglobin's cooperative oxygen binding curve has a Hill coefficient of about 2.8, which is why it can load and unload oxygen so much more efficiently than non-cooperative carriers like myoglobin.