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- W2029222376 endingPage "1310" @default.
- W2029222376 startingPage "1304" @default.
- W2029222376 abstract "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." @default.
- W2029222376 created "2016-06-24" @default.
- W2029222376 creator A5050049504 @default.
- W2029222376 creator A5065633302 @default.
- W2029222376 date "2013-09-23" @default.
- W2029222376 modified "2023-10-07" @default.
- W2029222376 title "Simulations Suggest Possible Novel Membrane Pore Structure" @default.
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- W2029222376 doi "https://doi.org/10.1021/la402727a" @default.
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