P
Peter L. Davies
Researcher at Queen's University
Publications - 282
Citations - 17259
Peter L. Davies is an academic researcher from Queen's University. The author has contributed to research in topics: Antifreeze protein & Ice binding. The author has an hindex of 70, co-authored 280 publications receiving 15854 citations. Previous affiliations of Peter L. Davies include Georgia Institute of Technology & Case Western Reserve University.
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Journal ArticleDOI
Antifreeze proteins of teleost fishes.
TL;DR: The remarkable diversity of antifreeze types and their seemingly haphazard phylogenetic distribution suggest that these proteins might have evolved recently in response to sea level glaciation occurring just 1-2 million years ago in the northern hemisphere and 10-30 million years old around Antarctica.
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Biochemistry of fish antifreeze proteins.
Peter L. Davies,Choy L. Hew +1 more
TL;DR: It is suggested that type I AFP binds preferentially to the prism faces of ice crystals as a result of interactions between the helix macrodipole and the dipoles on the water molecules in the ice lattice.
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Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein
TL;DR: 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 from the beetle Tenebrio molitor perhaps the most regular protein structure yet observed.
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β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
Steffen P. Graether,Steffen P. Graether,Michael J. Kuiper,Stéphane M. Gagné,Virginia K. Walker,Zongchao Jia,Brian D. Sykes,Peter L. Davies +7 more
TL;DR: 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.
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Antifreeze proteins: an unusual receptor–ligand interaction
Zongchao Jia,Peter L. Davies +1 more
TL;DR: It now seems probable that van der Waals and hydrophobic interactions make a significant contribution to the enthalpy of adsorption.