Certain plants, insects, and fish living in cold environments prevent tissue damage due to freezing by producing antifreeze proteins or antifreeze glycoproteins that inhibit ice growth below the normal equilibrium freezing point of water in a noncolligative fashion. In polar fish these macromolecules, taking into account their structural characteristics, are grouped into three broad classes, namely Type I, Type II, and Type III. In this paper we report the results of our studies on the stereospecific binding of sea raven, a Type II antifreeze protein (AFP) to (111) hexagonal bipyramidal faces of ice. Earlier studies of Type I and Type III AFPs have shown that stereospecific binding of these proteins, recognizing specific planes of ice, is essential for their noncolligative antifreeze point depression. Moreover, as it has been shown for the AFT of Type I, this binding also occurs along specific vectors on these planes and also is enantioselective, distinguishing between the mirror related directions. In this study we will show, by using molecular modeling, that the fold of Type II AFP could facilitate a stereospecific mode of interaction with (111) planes of ice. Similar to Type I AFP, preferential directionality of binding was also observed in the simulations.
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