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Binding mechanism and antifreeze function According to the structure and function study on the antifreeze protein from the fish winter flounder, the antifreeze mechanism of the type-I AFP molecule was shown to be due to the binding to an ice nucleation structure in a zipper-like fashion through hydrogen bonding of the hydroxyl groups of its four Thr residues to the oxygens along the The above mechanism can be used to elucidate the structure-function relationship of other antifreeze proteins with the following two common features: recurrence of a Thr residue (or any other polar amino acid residue whose side-chain can form a hydrogen bond with water) in an 11-amino-acid period along the sequence concerned, and a high percentage of an Ala residue component therein

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