A model for binding of an antifreeze polypeptide to ice

A model for binding of an antifreeze polypeptide to ice

A model is proposed, based on recent peptide analog and ice crystal etching studies, whereby an alanine-rich, alpha-helical antifreeze polypeptide (AFP) from the winter flounder inhibits the growth of ice crystals by hydrogen bonding of Thr, Asn, and Asp side chains in a specific pattern to the [202...

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Veröffentlicht in:Biophysical journal 1992-12, Vol.63 (6), p.1659-1662
Hauptverfasser: Wen, D., Laursen, R.A.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Animals
Antifreeze Proteins
Binding Sites
Biological and medical sciences
Biophysical Phenomena
Biophysics
Fishes
Freezing
Fundamental and applied biological sciences. Psychology
Glycoproteins - chemistry
Hydrogen Bonding
Ice
Interactions. Associations
Intermolecular phenomena
Models, Molecular
Molecular biophysics
Molecular Sequence Data
Protein Structure, Secondary
Thermodynamics
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Zusammenfassung:A model is proposed, based on recent peptide analog and ice crystal etching studies, whereby an alanine-rich, alpha-helical antifreeze polypeptide (AFP) from the winter flounder inhibits the growth of ice crystals by hydrogen bonding of Thr, Asn, and Asp side chains in a specific pattern to the [2021] hexagonal bipyramidal planes of ice. It is further suggested that this mode of binding is unidirectional, maximizing opportunities for packing of AFPs on the ice surface, and that ice crystal growth inhibition occurs by a two-step mechanism involving hydrogen bonding and hydrophobic interpeptide interactions.
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(92)81750-2