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Review
. 2002 Jul 29;357(1423):927-35.
doi: 10.1098/rstb.2002.1081.

Structure and function of antifreeze proteins

Peter L Davies  1 , Jason Baardsnes, Michael J Kuiper, Virginia K Walker
Affiliations
Review

Structure and function of antifreeze proteins

Peter L Davies et al. Philos Trans R Soc Lond B Biol Sci. .

Abstract

High-resolution three-dimensional structures are now available for four of seven non-homologous fish and insect antifreeze proteins (AFPs). For each of these structures, the ice-binding site of the AFP has been defined by site-directed mutagenesis, and ice etching has indicated that the ice surface is bound by the AFP. A comparison of these extremely diverse ice-binding proteins shows that they have the following attributes in common. The binding sites are relatively flat and engage a substantial proportion of the protein's surface area in ice binding. They are also somewhat hydrophobic -- more so than that portion of the protein exposed to the solvent. Surface-surface complementarity appears to be the key to tight binding in which the contribution of hydrogen bonding seems to be secondary to van der Waals contacts.

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