Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-1-3
pubmed:abstractText
Knowledge of the secondary structure of antifreeze peptides (AFPs) and glycopeptides (AFGPs) is crucial to understanding the mechanism by which these molecules inhibit ice crystal growth. A polyproline type II helix is perhaps the most widely accepted conformation for active AFGPs; however, random coil and alpha-helix conformations have also been proposed. In this report we present vibrational spectroscopic evidence that the conformation of AFGPs in solution is not random, not alpha-helical, and not polyproline type II. Comparison of AFGP amide vibrational frequencies with those observed and calculated for beta and gamma-turns in other peptides strongly suggests that AFGPs contain substantial turn structure. Computer-generated molecular models were utilized to compare gamma-turn, beta-turn, and polyproline II structures. The gamma-turn motif is consistent with observed amide frequencies and results in a molecule with planar symmetry with respect to the disaccharides. This intriguing conformation may provide new insight into the unusual properties of AFGPs.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-1168194, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-1262326, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-2009357, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-2185972, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-2194218, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-2300815, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-267952, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-3368002, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-3541539, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-3793370, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-5488456, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-5542001, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-5764871, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-6087734, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-6466773, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-651675, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-6614910, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-7066471, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-7228488, http://linkedlifedata.com/resource/pubmed/commentcorrection/8241413-7372583
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3495
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
985-91
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Evidence for a gamma-turn motif in antifreeze glycopeptides.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't