Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions

Andrew C. Doxey, Mahmoud W. Yaish, Marilyn Griffith, Brendan J. McConkey

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Antifreeze proteins (AFPs) are found in cold-adapted organisms and have the unusual ability to bind to and inhibit the growth of ice crystals. However, the underlying molecular basis of their ice-binding activity is unclear because of the difficulty of studying the AFP-ice interaction directly and the lack of a common motif, domain or fold among different AFPs. We have formulated a generic ice-binding model and incorporated it into a physicochemical pattern-recognition algorithm. It successfully recognizes ice-binding surfaces for a diverse range of AFPs, and clearly discriminates AFPs from other structures in the Protein Data Bank. The algorithm was used to identify a novel AFP from winter rye, and the antifreeze activity of this protein was subsequently confirmed. The presence of a common and distinct physicochemical pattern provides a structural basis for unifying AFPs from fish, insects and plants.

Original languageEnglish
Pages (from-to)852-855
Number of pages4
JournalNature Biotechnology
Volume24
Issue number7
DOIs
Publication statusPublished - Jul 2006

Fingerprint

Antifreeze Proteins
Ice
Carbon
Proteins
Fish
Pattern recognition
Crystallization
Insects
Fishes
Databases
Crystals

ASJC Scopus subject areas

  • Microbiology

Cite this

Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. / Doxey, Andrew C.; Yaish, Mahmoud W.; Griffith, Marilyn; McConkey, Brendan J.

In: Nature Biotechnology, Vol. 24, No. 7, 07.2006, p. 852-855.

Research output: Contribution to journalArticle

Doxey, Andrew C. ; Yaish, Mahmoud W. ; Griffith, Marilyn ; McConkey, Brendan J. / Ordered surface carbons distinguish antifreeze proteins and their ice-binding regions. In: Nature Biotechnology. 2006 ; Vol. 24, No. 7. pp. 852-855.
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