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Crystal structure of an antifreeze polypeptide and its mechanistic implications

Nature volume 333, pages 232–237 (1988)Cite this article

Abstract

The X-ray crystallographic structure of an antifreeze polypeptide from the fish winter flounder, has been determined at 2.5 Å by an analysis of the Patter son function. This is the first report of a polypeptide of this size that is a single α-helix. A proposed mechanism of antifreeze binding to ice surfaces is given which requires: first, that the dipole moment from the helical structure dictates the preferential alignment of the peptide to the c-axis of ice nuclei; second, amphiphilicity of the helix; and third, torsional freedom of the side chains to facilitate hydrogen bonding to ice surfaces.

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Authors and Affiliations

  1. Biocrystallography Laboratory, VA Medical Center, PO Box 12055, Pittsburgh, Pensylvania, 15240

    D. S. C. Yang & M. Sax

  2. Department of Crystallography, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    D. S. C. Yang & M. Sax

  3. Research Institute, Hospital for Sick Children, Toronto

    A. Chakrabartty & C. L. Hew

  4. Departments of Biochemistry and Clinical Biochemistry, University of Toronto, Toronto, M5G 1L5, Canada

    A. Chakrabartty & C. L. Hew

Authors
  1. D. S. C. Yang
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  2. M. Sax
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  3. A. Chakrabartty
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  4. C. L. Hew
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Yang, D., Sax, M., Chakrabartty, A. et al. Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature 333, 232–237 (1988). https://doi.org/10.1038/333232a0

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