%0 Journal Article %A Vácha, Robert %A Frenkel, Daan %D 2014 %T Simulations Suggest Possible Novel Membrane Pore Structure %U https://acs.figshare.com/articles/journal_contribution/Simulations_Suggest_Possible_Novel_Membrane_Pore_Structure/2324371 %R 10.1021/la402727a.s001 %2 https://acs.figshare.com/ndownloader/files/3962002 %K MARTINI force field %K metastable pores %K microsecond time scale %K peptide %K formation %K membrane plane %K simulations show %K membrane pore %K Possible Novel Membrane Pore StructureAmphiphilic proteins %K toroidal pores %X 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. %I ACS Publications