Home▸Medicine & Biophysics▸Heat-Shock Chaperone Protein Folding Simulator

🌡️ Heat-Shock Chaperone Protein Folding Simulator

See how Hsp70 and Hsp90 chaperones bind partially-folded proteins to prevent aggregation under thermal stress, and what happens when rising temperature pushes chaperone demand past supply.

Medicine & Biophysics3DModerate60 FPS

The simulation shows a population of proteins destabilizing under rising temperature while Hsp70 and Hsp90 chaperones bind exposed hydrophobic patches to prevent aggregation, until chaperone demand exceeds available supply.

🔬 What It Demonstrates

🎮 How to Use

Raise the temperature slider to increase thermal stress and watch chaperones intervene in real time, and adjust the chaperone supply slider to see how much stress the system can absorb before aggregates begin forming.

💡 Did You Know?

Heat-shock proteins were discovered by accident in 1962 when a researcher accidentally overheated an incubator holding fruit fly larvae and noticed dramatic new patterns appear in their chromosomes.

⚙ Under the hood

See how Hsp70 and Hsp90 chaperones bind partially-folded proteins to prevent aggregation under thermal stress, and what happens when rising temperature pushes chaperone demand past supply.

cell biologyheat shock proteinsprotein foldingmolecular chaperoneshsp70hsp90proteostasiscellular stress response

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