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Cited by 313

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Structure and function of antifreeze proteins

Open access
Davies, Peter L., Baardsnes, Jason, Kuiper, Michael J., Walker, Virginia K.·2002·Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences

Abstract

High–resolution three–dimensional structures are now available for four of seven non–homologous fish and insect antifreeze proteins (AFPs). For each of these structures, the ice–binding site of the AFP has been defined by site–directed mutagenesis, and ice etching has indicated that the ice surface is bound by the AFP. A comparison of these extremely diverse ice–binding proteins shows that they have the following attributes in common. The binding sites are relatively flat and engage a substantial proportion of the protein's surface area in ice binding. They are also somewhat hydrophobic—more so than that portion of the protein exposed to the solvent. Surface–surface complementarity appears to be the key to tight binding in which the contribution of hydrogen bonding seems to be secondary to van der Waals contacts.

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Metadata

Authors
Davies, P. L., Baardsnes, J., Kuiper, M. J., & Walker, V. K.
Venue
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
Published
2002-07-29
Volume
357
Issue
1423
Pages
927-935
ISSN
  • 0962-8436 (ISSN-L)
  • 1471-2970
OpenAlex
W2148378265
Cited by
313
References
32
FWCI
2.38
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Structure and function of antifreeze proteins. https://app.cochat.ai/papers/10.1098/rstb.2002.1081
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Davies, P. L., Baardsnes, J., Kuiper, M. J., & Walker, V. K. (2002). Structure and function of antifreeze proteins. Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. https://doi.org/10.1098/rstb.2002.1081

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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