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. 2013 Feb 5;104(3):643–654. doi: 10.1016/j.bpj.2012.12.022

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© 2013 by the Biophysical Society.

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The average configuration of (a) interfacial alamethicin, (b) transmembrane alamethicin, (c) melittin, (d) KB1, (e) 18A, (f) interfacial ^KKpL₁₅, and (g) transmembrane ^KKpL₁₅ at n_P/n_L = 0.01 and χ = 0. The average helix contents calculated based on the structures from our simulations are: 85% for alamethicin, 80% for melittin, 84% for 18A, and 75% for ^KKpL₁₅, which are a little higher than the corresponding experimental values of 71–74% (84), 76% (84), 70–76% (76), and 65–75% (77). The structures do not change significantly with n_P/n_L or χ. The lines denote the hydrophobic boundary of the bilayers.