Averages of the fluorine-fluorine surface of contact in Ų.

<p>Averages of the fluorine-fluorine surface of contact in Ų.</p

Superstructure stability (top row) and typical equilibrated structures (bottom row) of the LX2 trimer, tetramer, pentamer and hexamer.

<p>Surrounding lipids are not shown for clarity. The pentamer and hexamer starting structures are not completely symmetric following energy minimization. Internal diameters (I.D.) are averaged values along the complete pore lumen. The color code is the same as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0166587#pone.0166587.g005" target="_blank">Fig 5</a>.</p

Initial rates of transport for alkali metal chlorides by LX2 at 100 nM.

<p>Initial rates of transport for alkali metal chlorides by LX2 at 100 nM.</p

Membrane Assembly and Ion Transport Ability of a Fluorinated Nanopore - Fig 1

<p><b>Structure representations</b> (a) Linear structure of the fluorinated 21-residue peptide LX2 under investigation, with 15 L-leucines (L) and 6 L-2, 2, 2-trifluoroethylglycine (F); (b) Axial wheel projection illustrating the amphiphilic fluorous/hydrophobic faces of LX2 α-helix; (c) Schematic representation of a tetrameric arrangement of LX2, showing in green the fluorinated faces of the four-helix bundle, and in red the hydrophobic contours.</p

Mass spectrum of LX2 obtained using MALDI mass spectrometry.

<p>Mass spectrum of LX2 obtained using MALDI mass spectrometry.</p

Self-assembly of LX2 dimers during MD simulations of 12 monomers.

<p>Fluorine atoms in green, carbon atoms from fluorinated amino acids in grey, peptide backbone in red and leucine residues in yellow. Lipids are shown in thin lines. Dimers are indicated by arrows.</p

Circular dichroism spectra of LX2

<p>Top: in HFIP at different concentrations; Bottom: using POPC/cholesterol (8:2) vesicles at different peptide/lipid ratios; Insert: Graph of molar ellipticity at 222 nm vs concentration.</p