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

John Spencer Evans

Research output: Contribution to journalReview article

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
DOIs
StatePublished - Mar 2003

Keywords

  • 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

Fingerprint Dive into the research topics of ''Apples' and 'oranges': Comparing the structural aspects of biomineral- and ice-interaction proteins'. Together they form a unique fingerprint.

  • Cite this