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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Biochim Biophys Acta. 2012 Dec 11;1828(3):1057–1065. doi: 10.1016/j.bbamem.2012.12.003

Figure 1. The key players in this study: a stiff β-barrel protein nanopore and lipids with various dimensionless shape parameters.

Figure 1

The panels indicate the wild-type FhuA (WT-FhuA) (A) and engineered FhuA ΔC/Δ4L proteins (B). The top and bottom panels show the side and extracellular views, respectively. FhuA ΔC/Δ4L protein nanopore was designed by deleting loops L3 (blue), L4 (magenta), L5 (gray), L11 (light green) and the first 160 amino acids (the cork domain, red) of the WT-FhuA protein. These large extracellular loops were replaced with the peptide linkers NSEGS (these linkers have similar color with the deleted loop); (C) A cartoon showing the geometrical shapes of lipids, their corresponding dimensionless shape parameter (S) as well as their phase of intermolecular association.