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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6
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pubmed:dateCreated |
2004-12-22
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pubmed:abstractText |
We have analyzed the secondary structure of spidroin proteins of I and II types, related to spiders of different species. We used standard methods of secondary structure prediction NNPREDICT and JPRED and also analyzed the occurrences of oligopeptides with a preferred secondary structure with the help of the OLIGON program. We have demonstrated that local segments of the polypeptide chain can adopt alpha- and beta-conformations as well as the left-handed helix of polyproline II type. Periodical patterns found in the amino acid distribution indicate that there is a possibility of development of a macroscopic order accompanied by local conformational transitions.
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pubmed:language |
rus
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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:issn |
0006-3029
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1147-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15612562-Amino Acid Sequence,
pubmed-meshheading:15612562-Animals,
pubmed-meshheading:15612562-Fibroins,
pubmed-meshheading:15612562-Insect Proteins,
pubmed-meshheading:15612562-Models, Molecular,
pubmed-meshheading:15612562-Molecular Sequence Data,
pubmed-meshheading:15612562-Protein Structure, Secondary,
pubmed-meshheading:15612562-Silk,
pubmed-meshheading:15612562-Species Specificity,
pubmed-meshheading:15612562-Spiders
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|
pubmed:articleTitle |
[An analysis of the secondary structure of spider spidroins I and II belonging to different species].
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pubmed:publicationType |
Letter,
Comparative Study,
English Abstract
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