Peptide and glycopeptide antifreezes from a variety of cold-water fishes cause ice single crystals grown from the melt to assume unusual and strikingly similar habits. The antifreezes inhibit growth on the prism faces but allow limited growth on the basal plane. As new layers are deposited on the basal plane, pyramidal surfaces develop on the outside of the crystal, and large hexagonal pits form within the basal plane. The pits are rotated 30 degrees with respect to the normal orientation of hexagonal ice crystals. Growth inhibition on the prism, pyramidal, and pit faces indicates that these faces contain sites of adsorption of the antifreeze molecules. Several properties of the antifreeze pits are consistent with (but do not prove) an origin of the pits at dislocations. The similarity of crystal habit imposed on ice by antifreezes with wide differences in composition and structure indicates a common mechanism.

Item Type:	Refereed Article
Keywords:	antifreeze protein, glycoprotein, ice, blodd, crystallization, fish, freezing
Research Division:	Chemical Sciences
Research Group:	Physical Chemistry (incl. Structural)
Research Field:	Structural Chemistry and Spectroscopy
Objective Division:	Expanding Knowledge
Objective Group:	Expanding Knowledge
Objective Field:	Expanding Knowledge in the Physical Sciences
Author:	Wilson, PW (Professor Peter Wilson)
ID Code:	105173
Year Published:	1989
Web of Science® Times Cited:	140
Deposited By:	Research Division
Deposited On:	2015-12-11
Last Modified:	2016-01-19
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