Journal article
Crystal structure of an antifreeze polypeptide and its mechanistic implications
Abstract
The X-ray crystallographic structure of an antifreeze polypeptide from the fish winter flounder, has been determined at 2.5 Å by an analysis of the Patter son function. This is the first report of a polypeptide of this size that is a single α-helix. A proposed mechanism of antifreeze binding to ice surfaces is given which requires: first, that the dipole moment from the helical structure dictates the preferential alignment of the peptide to the …
Authors
Yang DSC; Sax M; Chakrabartty A; Hew CL
Journal
Nature, Vol. 333, No. 6170, pp. 232–237
Publisher
Springer Nature
Publication Date
May 1988
DOI
10.1038/333232a0
ISSN
0028-0836