'Apples' and 'oranges'

Comparing the structural aspects of biomineral- and ice-interaction proteins

Research output: Contribution to journalArticle

Abstract

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
Volume8
Issue number1-2
DOIs
StatePublished - Mar 2003

Fingerprint

Ice
ice
proteins
Proteins
Minerals
minerals
interactions
trends
Hydrophobicity
hydrophobicity
helices
Conformations
coils

Keywords

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

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces and Interfaces

Cite this

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abstract = "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.",
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