Structure of a peptide antifreeze and mechanism of adsorption to ice

Research output: Contribution to journalArticlepeer-review

Abstract

Sequence studies of an α-helical peptide antifreeze isolated from winter flounder have revealed the presence of clusters of polar amino acids separated by long sequences of alanine. Most of the polar residues are threonine and aspartate and are separated by 4.5 Å, a repeat distance that also separates the oxygens in the ice lattice along the a-axis of an ice crystal. Such a lattice match suggests that the peptide binds to ice by means of hydrogen binding.

Original languageEnglish (US)
Pages (from-to)388-392
Number of pages5
JournalBBA - Protein Structure
Volume495
Issue number2
DOIs
StatePublished - Dec 20 1977

ASJC Scopus subject areas

  • Medicine(all)

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