Source:http://linkedlifedata.com/resource/pubmed/id/17029930
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2-3
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| pubmed:dateCreated |
2006-10-10
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| pubmed:abstractText |
Conformational studies of synthetic peptides corresponding to the pore-forming regions of voltage-gated sodium channels show a high tendency for beta-sheet conformation when interacting with lipid vesicles, as revealed by circular dichroism and infrared spectroscopy. These observations have guided our choice of possible molecular models for the P-region peptide of domain II of voltage-gated sodium channels: three alternative beta-hairpins, with differing turn assignments, or an alpha-helical hairpin. After generation of models by distance geometry-based methods, molecular dynamics (MD) simulations were run. in the absence of explicit solvent molecules but employing three different dielectric constants, to explore possible conformational preferences. The simulations in the different dielectric environments suggest that a 4-residue turn with the sequence LCGE yields more stable beta-hairpins. The MD results suggest that the SS1 part of the peptide may be more stable as an alpha-helix, whereas the SS2 part tends to adopt a beta-conformation.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0301-4622
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
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| pubmed:volume |
69
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
221-32
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| pubmed:dateRevised |
2009-9-29
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| pubmed:year |
1997
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| pubmed:articleTitle |
Secondary structure of an isolated P-region from the voltage-gated sodium channel: a molecular modelling/dynamics study.
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| pubmed:affiliation |
UMR 6522 CNRS-Université de Rouen (IFRMP 23), Boulevard M. de Broglie, Mont-Saint-Aigman 76821, France.
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| pubmed:publicationType |
Journal Article
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