Linked Life Data

2009357

Source:http://linkedlifedata.com/resource/pubmed/id/2009357

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-5-7
pubmed:abstractText
The noncolligative peptide and glycopeptide antifreezes found in some cold-water fish act by binding to the ice surface and preventing crystal growth, not by altering the equilibrium freezing point of the water. A simple crystal growth and etching technique allows determination of the crystallographic planes where the binding occurs. In the case of elongated molecules, such as the alpha-helical peptides in this report, it also allows a deduction of the molecular alignment on the ice surface. The structurally similar antifreeze peptides from winter flounder (Pseudopleuronectes americanus) and Alaskan plaice (Pleuronectes quadritaberulatus) adsorb onto the (2021) pyramidal planes of ice, whereas the sculpin (Myoxocephalus scorpius) peptide adsorbs on (2110), the secondary prism planes. All three are probably aligned along (0112). These antifreeze peptides have 11-amino acid sequence repeats ending with a polar residue, and each repeat constitutes a distance of 16.5 A along the helix, which nearly matches the 16.7 A repeat spacing along (0112) in ice. This structural match is undoubtedly important, but the mechanism of binding is not yet clear. The suggested mechanism of growth inhibition operates through the influence of local surface curvature upon melting point and results in complete inhibition of the crystal growth even though individual antifreeze molecules bind at only one interface orientation.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3495
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
409-18
pubmed:dateRevised
2010-9-10
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes.
pubmed:affiliation
National Center for Atmospheric Research, Boulder, Colorado 80307.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.