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Science 21 October 2005:
Vol. 310. no. 5747, p. 461
DOI: 10.1126/science.1115145
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Brevia

Glycine-Rich Antifreeze Proteins from Snow Fleas

Laurie A. Graham1 and Peter L. Davies1,2*

We purified antifreeze proteins from winter-active snow fleas, Hypogastrura harveyi. These 6.5- and 15.7-kilodalton thermolabile proteins are glycine-rich (45% of the residues), and the short isoform is composed of the tripeptide repeat Gly-X-X. This makes them very different from other antifreeze proteins, including two from insects, suggesting independent adaptation to freezing environments.

1 Department of Biochemistry.
2 Protein Function Discovery Group, Queen's University, Kingston, ON K7L 3N6, Canada.

* To whom correspondence should be addressed. E-mail: daviesp{at}post.queensu.ca

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Direct Visualization of Spruce Budworm Antifreeze Protein Interacting with Ice Crystals: Basal Plane Affinity Confers Hyperactivity.
N. Pertaya, C. B. Marshall, Y. Celik, P. L. Davies, and I. Braslavsky (2008)
Biophys. J. 95, 333-341
   Abstract »    Full Text »    PDF »
Fluorescence Microscopy Evidence for Quasi-Permanent Attachment of Antifreeze Proteins to Ice Surfaces.
N. Pertaya, C. B. Marshall, C. L. DiPrinzio, L. Wilen, E. S. Thomson, J. S. Wettlaufer, P. L. Davies, and I. Braslavsky (2007)
Biophys. J. 92, 3663-3673
   Abstract »    Full Text »    PDF »
Structural Modeling of Snow Flea Antifreeze Protein.
F.-H. Lin, L. A. Graham, R. L. Campbell, and P. L. Davies (2007)
Biophys. J. 92, 1717-1723
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)