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Philos Trans R Soc Lond B Biol Sci. 2002 Jul 29;357(1423):927-35.

Structure and function of antifreeze proteins.

Author information

  • 1Department of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6. daviesp@post.queensu.ca

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.

PMID:
12171656
PMCID:
PMC1692999
DOI:
10.1098/rstb.2002.1081
[PubMed - indexed for MEDLINE]
Free PMC Article
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