@article{7bf134a647cc49caafceab85174ef05c,
title = "Structure of a peptide antifreeze and mechanism of adsorption to ice",
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 {\AA}, 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.",
author = "Devries, {Arthur L.} and Yuan Lin",
note = "Funding Information: The fact that the groups of polar residues with 4.5 A spacings are separated by 5 to 7 non-polar alanine residues may be significant, because if a continuous 4.5 A repeat distance were present it could serve as a template for ice formation. The long sequences of alanines probably exist to ensure that each 4.5 A spacing is separated from another so that it would not be possible for them to function as an ice nucleator. We thank Mr. Pete Segrist of Scripps Clinic for performing the Edman degradation of peptide 3 on the automatic sequenator. This study was supported by grants from NSF (OPP 74-07917) and NIH (GM 21127).",
year = "1977",
month = dec,
day = "20",
doi = "10.1016/0005-2795(77)90395-6",
language = "English (US)",
volume = "495",
pages = "388--392",
journal = "BBA - Protein Structure",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",
}