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Structure, function and evolution of antifreeze proteins

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Abstract

Antifreeze proteins bind to ice crystals and modify their growth. These proteins show great diversity in structure, and they have been found in a variety of organisms. The ice-binding mechanisms of antifreeze proteins are not completely understood. Recent findings on the evolution of antifreeze proteins and on their structures and mechanisms of action have provided new understanding of these proteins in different contexts. The purpose of this review is to present the developments in contrasting research areas and unite them in order to gain further insight into the structure and function of the antifreeze proteins.

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Authors and Affiliations

  1. NRC Institute for Marine Biosciences, 1411 Oxford St., B3H 3Z1, Halifax, Nova Scotia, Canada

    K. V. Ewart

  2. Research Institute, Hospital for Sick Children and Departments of Clinical Biochemistry and Biochemistry, University of Toronto, M5G 1L5, Toronto, Ontario, Canada

    Q. Lin & C. L. Hew

Authors
  1. K. V. Ewart
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  2. Q. Lin
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  3. C. L. Hew
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Corresponding author

Correspondence to C. L. Hew.

Additional information

Received 2 September 1998; received after revision 21 October 1998; accepted 2 November 1998

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Ewart, K., Lin, Q. & Hew, C. Structure, function and evolution of antifreeze proteins. CMLS, Cell. Mol. Life Sci. 55, 271–283 (1999). https://doi.org/10.1007/s000180050289

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  • DOI: https://doi.org/10.1007/s000180050289

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