Home▸Medicine & Biophysics▸Allosteric Enzyme Regulation and Cooperativity Simulator

🧬 Allosteric Enzyme Regulation and Cooperativity Simulator

Compare sigmoidal allosteric enzyme kinetics against classic Michaelis-Menten curves and see how binding an activator or inhibitor at a regulatory site reshapes the velocity-versus-substrate relationship.

Medicine & Biophysics3DModerate60 FPS

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.

🔬 What It Demonstrates

🎮 How to Use

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.

💡 Did You Know?

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.

⚙ Under the hood

biochemistryallosteric regulationenzyme kineticscooperativitymichaelis-mentenhemoglobinmolecular biologyprotein structure

3D · Three.js / WebGL renderer · 60 FPS target · runs fully client-side, no install