'Apples' and 'oranges': Comparing the structural aspects of biomineral- and ice-interaction proteins

John Spencer Evans

    Research output: Contribution to journalReview articlepeer-review


    The title of this review describes structural comparisons of protein classes whose task is to identify and interact with biological solids (minerals and ice). To date, the following trends have been noted: (1) biomineral-interaction proteins typically adopt unfolded, open conformations, and, where mineral binding motifs have been identified, these sequences exhibit structural trends towards extended, random coil, or other unstable secondary structures; (2) ice-interaction proteins typically adopt folded structures, featuring stable secondary structure preferences (α-helix, β-sheet, β-helix, etc.) and stable, planar ice binding motifs that exploit hydrophobicity and van der Waals' interactions for ice binding.

    Original languageEnglish (US)
    Pages (from-to)48-54
    Number of pages7
    JournalCurrent Opinion in Colloid and Interface Science
    Issue number1
    StatePublished - Mar 2003


    • Biomineralization
    • Ice antifreeze
    • Ice nucleation
    • Inorganic
    • Interfaces
    • Minerals
    • Polypeptides
    • Secondary structure

    ASJC Scopus subject areas

    • Surfaces and Interfaces
    • Physical and Theoretical Chemistry
    • Polymers and Plastics
    • Colloid and Surface Chemistry


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