Characteristics of Antifreeze Proteins

  • Erlend KristiansenEmail author


Antifreeze proteins (AFPs) and antifreeze glycoproteins (AFGPs) have evolved independently in a variety of life forms and are characterized as a group only by their common ability to prevent existing ice crystals from growing in supercooled solutions. This chapter attempts to give a broad overview of some of the shared and unique characteristics of AF(G)Ps found in polar fish and freeze-avoiding arthropods. These include structural, evolutionary, regulatory and operational characteristics. Structurally similar AF(G)Ps are found within distantly related groups, and different forms are found in more related groups. Today’s phylogenetic patterns of distribution are the results of several evolutionary processes. Expression of AF(G)Ps in fish and in insects are often influenced by environmental cues that signal the onset of winter, that act on hormonal control mechanisms of gene expression. Within species, there are large number of genes coding for AF(G)Ps, and these are often arranged in tandem. In many species of fish and insects, the genes themselves are constructed by multiple repeats in sequence, resulting in many isoforms of mature AF(G)Ps, some constructed from a varying number of repeat segments. Several similar helical secondary structures are found in unrelated mature AF(G)Ps, implying that these structures are effective general scaffolds for ice binding. The ice-binding surface sites of these proteins are located at planar regions of their surface and apparently structure water in an ice-like manner to secure effective binding to the ice lattice. Thus, AF(G)Ps comprise a diverse group that have many general characteristics in common, but also others that set them apart.


Antifreeze protein Antifreeze glycoprotein Structure Ice binding Ice-binding site Protein structure Isoforms 


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Authors and Affiliations

  1. 1.NTNU University LibraryTrondheimNorway

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