Ice crystal front
Bound AFGP molecule
Drag to orbit · click ice to bind a protein
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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.