# Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein

@article{Liou2000MimicryOI,
title={Mimicry of ice structure by surface hydroxyls and water of a $\beta$-helix antifreeze protein},
author={Yih-Cherng Liou and Ante Tocilj and Peter L. Davies and Zongchao Jia},
journal={Nature},
year={2000},
volume={406},
pages={322-324}
}
Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition. [...] Key Result Not only are the 12-amino-acid loops almost identical in the backbone, but also the conserved side chains are positioned in essentially identical orientations, making this AFP perhaps the most regular protein structure yet observed. The protein has almost no hydrophobic core but is stabilized by numerous disulphide and hydrogen bonds.Expand
363 Citations

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#### References

SHOWING 1-10 OF 27 REFERENCES
β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
The solution structure of spruce budworm AFP is reported and its ice-binding properties are characterized; the 9-kDa AFP is a β-helix with a triangular cross-section and rectangular sides that form stacked parallel β-sheets; a fold which is distinct from the three known fish AFP structures. Expand
Ice-binding structure and mechanism of an antifreeze protein from winter flounder
• Chemistry, Medicine
• Nature
• 1995
An ice-binding model is proposed that accounts for the binding specificity of the antifreeze protein along the <011¯2> axes of the {202¯1} ice planes1. Expand
Folding and structural characterization of highly disulfide-bonded beetle antifreeze protein produced in bacteria.
• Y. Liou, +4 authors P. Davies
• Chemistry, Medicine
• Protein expression and purification
• 2000
NMR analysis and secondary structure predictions agree with the CD data and are consistent with a beta-helix model proposed for the antifreeze on the basis of its 12-amino-acid repeating structure and presumptive disulfide bond arrangement. Expand
Mapping of disulfide bridges in antifreeze proteins from overwintering larvae of the beetle Dendroides canadensis.
• Chemistry, Medicine
• Biochemistry
• 1998
This study demonstrated that all of the 16 Cys residues in the Dendroides AFPs are disulfide bridged, and the location of cysteines every six residues throughout their length is essential to understanding the structure of these AFPs. Expand
Adsorption to ice of fish antifreeze glycopeptides 7 and 8.
• Chemistry, Medicine
• Biophysical journal
• 1993
Experimental results show that fish antifreeze glycopeptides 8 and 7 bond onto ice prism planes aligned along a-axes, and inhibit crystal growth on prism planes and on surfaces close to that orientation, explaining why the chemical adsorption is virtually irreversible and the crystal growth can be stopped virtually completely. Expand
Structure and Evolution of Parallel β-Helix Proteins
• Biology
• 1998
It is suggested that the stacking of the coils and the unusual near perpendicular junction of PB2 and PB3 make the parallel β-helix fold especially likely to maintain similar main chain conformations during divergent evolution even after all vestige of similarity in primary structure has vanished. Expand
A complex family of highly heterogeneous and internally repetitive hyperactive antifreeze proteins from the beetle Tenebrio molitor.
• Biology, Medicine
• Biochemistry
• 1999
Genomic Southern blots suggest there may be 30-50 tightly linked copies of the gene, which is a signature consistently seen with unrelated fish antifreeze protein genes, and one that has been associated with the need to rapidly increase gene product in response to climate change. Expand
Structure and evolution of parallel beta-helix proteins.
• Medicine
• Journal of structural biology
• 1998
It is suggested that the stacking of the coils and the unusual near perpendicular junction of PB2 and PB3 make the parallel beta-helix fold especially likely to maintain similar main chain conformations during divergent evolution even after all vestige of similarity in primary structure has vanished. Expand
Crystal structure of a bovine neurophysin II dipeptide complex at 2.8 A determined from the single-wavelength anomalous scattering signal of an incorporated iodine atom.
• L. Chen, +5 authors B. Wang
• Chemistry, Medicine
• Proceedings of the National Academy of Sciences of the United States of America
• 1991
The crystal structure of a dipeptide complex of bovine neurophysin II has been solved at 2.8 A resolution solely by using single-wavelength anomalous scattering data from a single iodinatedExpand
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
• Biology, Medicine
• Science
• 1994
The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a modelExpand