rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
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pubmed:dateCreated |
1994-1-3
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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.
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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
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0006-3495
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
65
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
985-91
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8241413-Amino Acid Sequence,
pubmed-meshheading:8241413-Animals,
pubmed-meshheading:8241413-Antifreeze Proteins,
pubmed-meshheading:8241413-Biophysical Phenomena,
pubmed-meshheading:8241413-Biophysics,
pubmed-meshheading:8241413-Carbohydrate Sequence,
pubmed-meshheading:8241413-Fishes,
pubmed-meshheading:8241413-Freezing,
pubmed-meshheading:8241413-Glycoproteins,
pubmed-meshheading:8241413-Models, Molecular,
pubmed-meshheading:8241413-Molecular Sequence Data,
pubmed-meshheading:8241413-Molecular Structure,
pubmed-meshheading:8241413-Protein Conformation,
pubmed-meshheading:8241413-Protein Structure, Secondary,
pubmed-meshheading:8241413-Spectrophotometry, Infrared,
pubmed-meshheading:8241413-Spectrum Analysis, Raman
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pubmed:year |
1993
|
pubmed:articleTitle |
Evidence for a gamma-turn motif in antifreeze glycopeptides.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|