Letter Published: 01 June 1995 Ice-binding structure and mechanism of an antifreeze protein from winter flounder F. Sicheri1 & D. S. C. Yang1,2  Nature volume 375, pages 427–431 (1995)Cite

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crystal structure at 1.5 Å resolution of a lone α-helical antifreeze protein from winter flounder, which provides a detailed look at its icebinding features. These consist of four repeated

ice-binding motifs, the side chains of which are inherently rigid or restrained by pair-wise side-chain interactions to form a flat binding surface. Elaborate amino- and carboxy-terminal cap

structures are also present, which explain the protein's rich α-helical content in solution. We propose an ice-binding model that accounts for the binding specificity of the antifreeze

protein along the <011¯2> axes of the {202¯1} ice planes1.

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by others Polyproline type II helical antifreeze proteins are widespread in Collembola and likely originated over 400 million years ago in the Ordovician Period Article Open access 01 June

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Adsorption of ice-binding proteins onto whole ice crystal surfaces does not necessarily confer a high thermal hysteresis activity Article Open access 14 September 2022 References Knight, C.

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Author informationAuthors and Affiliations Department of Biochemistry, Faculty of Health Science, McMaster University, Hamilton, Ontario, L8N 3Z5, Canada

F. Sicheri & D. S. C. Yang

BioCrystallography Laboratory, VA Medical Center, PO Box 12055, Pittsburgh, Pennsylvania, 15240, USA

D. S. C. Yang

AuthorsF. SicheriView author publications You can also search for this author inPubMed Google Scholar

D. S. C. YangView author publications You can also search for this author inPubMed Google Scholar

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About this articleCite this article Sicheri, F., Yang, D. Ice-binding structure and mechanism of an antifreeze protein from winter flounder. Nature 375, 427–431 (1995).

https://doi.org/10.1038/375427a0

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Received: 16 February 1995

Accepted: 06 April 1995

Issue Date: 01 June 1995

DOI: https://doi.org/10.1038/375427a0

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