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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1990-10-12
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pubmed:abstractText |
The structures of four peptides corresponding to parts of the coeliac-activating protein A-gliadin were studied by structure prediction and c.d. spectroscopy. Three of the peptides corresponded to parts of the coeliac-activating N-terminal region (residues 3-55, 3-19 and 39-45) and contained two tetrapeptide motifs common to all coeliac-active regions (Pro-Ser-Gln-Gln and Gln-Gln-Gln-Pro). The Pro-Ser-Gln-Gln sequence was also present in the fourth peptide, on the basis of the C-terminal part of the molecule (211-217). These studies showed that beta-reverse turns were the predominant structural feature in all peptides and were predominantly of type I/III in two of the N-terminal peptides and type II in the C-terminal peptide. These turns form when the peptide is dissolved in solvents of low dielectric constant (trifluoroethanol) and high dielectric constant (water and iso-osmotic saline), although their presence in the N-terminal peptides may be masked in the latter solvents due to equilibrium with a poly-L-proline II structure favoured at lower temperatures.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-2456075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-2659519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-2719660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-2865874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3203684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3233285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3335296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-354496,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3705771,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3768484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3896269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-3991697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-5016973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-6183341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-6381246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-6491604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-6524078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-6589619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-6698719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-696813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-7295645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-7378550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2400392-82446
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
313-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2400392-Amino Acid Sequence,
pubmed-meshheading:2400392-Antigens,
pubmed-meshheading:2400392-Celiac Disease,
pubmed-meshheading:2400392-Circular Dichroism,
pubmed-meshheading:2400392-Ethylene Glycols,
pubmed-meshheading:2400392-Gliadin,
pubmed-meshheading:2400392-Molecular Sequence Data,
pubmed-meshheading:2400392-Peptide Fragments,
pubmed-meshheading:2400392-Plant Proteins,
pubmed-meshheading:2400392-Protein Conformation,
pubmed-meshheading:2400392-Solvents,
pubmed-meshheading:2400392-Structure-Activity Relationship,
pubmed-meshheading:2400392-Temperature,
pubmed-meshheading:2400392-Trifluoroethanol
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pubmed:year |
1990
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pubmed:articleTitle |
Conformational studies of peptides corresponding to the coeliac-activating regions of wheat alpha-gliadin.
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pubmed:affiliation |
AFRC Institute of Arable Crops Research, Rothamsted Experimental Station, Harpenden, Herts., U.K.
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pubmed:publicationType |
Journal Article
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