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231224s2014 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1021/la402727a
|2 doi
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|a pubmed24n0770.xml
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|a DE-627
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| 041 |
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|a eng
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| 100 |
1 |
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|a Vácha, Robert
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Simulations suggest possible novel membrane pore structure
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|c 2014
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 21.10.2014
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|a Date Revised 11.02.2014
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Amphiphilic proteins and peptides can induce the formation of stable and metastable pores in membranes. Using coarse-grained simulations, we have studied the factors that affect structure of peptide-stabilized pores. Our simulations are able to reproduce the formation of the well-known barrel-stave or toroidal pores, but in addition, we find evidence for a novel "double-belt" pore structure: in this structure the peptides that coat the membrane pore are oriented parallel to the membrane plane. To check the predictions of our coarse-grained model, we have performed more detailed simulations, using the MARTINI force field. These simulations show that the double-belt structure is stable up to at least the microsecond time scale
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| 650 |
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|a Journal Article
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| 650 |
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|a Research Support, Non-U.S. Gov't
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| 650 |
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7 |
|a Apolipoprotein A-I
|2 NLM
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| 650 |
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7 |
|a Membrane Lipids
|2 NLM
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| 650 |
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7 |
|a Peptides
|2 NLM
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| 650 |
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7 |
|a Phospholipids
|2 NLM
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| 700 |
1 |
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|a Frenkel, Daan
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 30(2014), 5 vom: 11. Feb., Seite 1304-10
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|x 1520-5827
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|g volume:30
|g year:2014
|g number:5
|g day:11
|g month:02
|g pages:1304-10
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