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Antifreeze Proteins: Blocking Ice Crystal Growth (2D)

A 2D cross-section of an ice-water interface pinned by adsorbed antifreeze glycoprotein molecules — pan and zoom the growth front, click to bind a protein, and watch the thermal hysteresis gap grow with concentration, contrasted against simple colligative antifreeze.

Biology2DModerate60 FPS📱 Mobile-adapted⇄ 3D version
antifreeze-glycoprotein-ice-blocking ↗ Open standalone

A simplified 2D cross-section of the ice-water interface shows how antifreeze glycoproteins actually work: not by colligative freezing-point depression like ethylene glycol, but by adsorbing onto the growing ice surface and pinning it locally through Kelvin-effect curvature. Pan and zoom the interface, click anywhere along it to bind a protein by hand, and watch the front bulge forward between pinned sites while the live thermal hysteresis readout — the true gap between the melting point and the depressed freezing point — widens as concentration and binding-site density increase.

⚙ Under the hood

A 2D cross-section of an ice-water interface pinned locally by adsorbed antifreeze glycoprotein molecules via the Kelvin-effect curvature mechanism, with a live thermal-hysteresis-gap readout comparable against simple colligative antifreeze.

antifreeze-proteinthermal-hysteresisice-adsorptioncryobiologynew-year

2D · HTML5 Canvas 2D · 60 FPS target · runs fully client-side, no install

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