A natural variant of type I antifreeze protein with four ice-binding repeats is a particularly potent antifreeze-Reference-Cited by-同舟云学术

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A natural variant of type I antifreeze protein with four ice-binding repeats is a particularly potent antifreeze

Published:1996-06 Issue:6 Volume:5 Page:1150-1156
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Chao Heman,Hodges Robert S.,Kay Cyril M.,Gauthier Sherry Y.,Davies Peter L.

Funder

Medical Research Council of Canada

Protein Engineering Network of Centres of Excellence

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560050617/fullpdf

Reference27 articles.

1. Structural studies on the freezing point-depressing protein of the winter flounde Pseudopleuronectes americanus;Ananthanarayanan;Biochem Biophys Res Commun,1977

2. Competing interactions contributing to alpha-helical stability in aqueous solution;Bodkin;Protein Sci,1995

3. The effect of enhanced alpha-helicity on the activity of a winter flounder antifreeze polypeptide;Chakrabartty;Eur J Biochem,1991

4. Determination of the helix and forms of proteins in aqueous solution by circular dichroism;Chen;Biochemistry,1974

5. Energy optimized structure of antifreeze protein and its binding mechanism;Chou;J Mot Biol,1992

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2. Frost fighters: unveiling the potential of microbial antifreeze proteins in biotech innovation;Journal of Applied Microbiology;2024-06

3. Protein engineering of antifreeze proteins reveals that their activity scales with the area of the ice‐binding site;FEBS Letters;2022-12-12

4. Protein engineering shows antifreeze activity scales with ice-binding site area;2022-09-07

5. Molecular simulation -based research on antifreeze peptides: advances and perspectives;Journal of Future Foods;2022-09

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