The structural types of AFP determine their ability to bind to specific crystallographic ice planes. This binding occurs through a region, known as the ice-binding site (IBS), on the AFP. The IBS is believed to organize water molecules adjacent to AFP into a conformation that mimics the lattice arrangement found in ice molecular structure, but without inducing actual ice formation (Kondo, 2012). By pre-arranging these water molecules into an ice-like pattern, AFPs effectively prepare their binding interface to complement a specific ice plane (Eskandari et al., 2020). The IBS then aligns with a corresponding plane on the ice surface upon encountering an ice crystal. The molecular complementarity between the water molecule arrangement at the IBS and the atomic structure of the targeted ice plane facilitates this attachment. Different AFPs exhibit different binding preferences depending on their structures. For instance, Type 1 AFPs from the winter flounder preferentially bind to the pyramidal and secondary prism planes of ice, whereas hyperactive AFPs from the Antarctic bacterium _Flavobacterium frigoris_ PS1 target the basal plane of ice crystals (Kim et al., 2017). These matchings replace water binding that causes further ice crystal growth at the site and enables the AFP to selectively adhere to ice planes (Eskandari et al., 2020).