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Philosophical Transactions of the Royal Society B: Biological Sciences logoLink to Philosophical Transactions of the Royal Society B: Biological Sciences
. 2002 Jul 29;357(1423):927–935. doi: 10.1098/rstb.2002.1081

Structure and function of antifreeze proteins.

Peter L Davies 1, Jason Baardsnes 1, Michael J Kuiper 1, Virginia K Walker 1
PMCID: PMC1692999  PMID: 12171656

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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