Antifreeze Proteins: Blocking Ice Crystal Growth (3D)
A 3D ice crystal growth front pinned locally by adsorbed antifreeze glycoprotein molecules — watch the Kelvin-effect curvature at each bound site create a real thermal hysteresis gap that widens with protein concentration, and compare it against simple colligative freezing-point depression.
Antifreeze glycoproteins in polar fish and overwintering insects protect tissue from freezing not by simple colligative freezing-point depression, but by binding directly onto growing ice crystal faces and pinning the growth front through a curvature-driven (Kelvin/Gibbs–Thomson) mechanism. This 3D simulation grows a real ice front around a disc, pins it locally at adsorbed-protein sites, and reads out the resulting thermal hysteresis gap — the real, measurable difference between the melting point and the depressed freezing point — live as you change protein concentration, binding-site density, undercooling, and the growth kinetics, or switch to a colligative-antifreeze comparison mode to see why that gap disappears.
A 3D ice crystal growth front 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.
3D · Three.js / WebGL renderer · 60 FPS target · runs fully client-side, no install