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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Mol Microbiol. 2011 Apr 27;80(6):1496–1515. doi: 10.1111/j.1365-2958.2011.07662.x

Figure 2. The C-terminal portion of TP0326 forms a β-barrel.

Figure 2

(A) Tryptophan fluorescence emission spectra of unfolded 326βB and OmpG and folded forms in 0.5% DDM and 1% OG micelles, respectively. (B) CD spectra of folded 326βB (5 μM) and OmpG (2.6 μM) in DDM and OG buffer, respectively. (C) Heat-modifiability of folded E. coli BamA, OmpG, 326βB, and 326P1-4+. Proteins were stained with GelCode® Blue following SDS-PAGE with (+) or without (-) boiling in sample buffer (SB). (D) T. pallidum samples were dissolved in SB without (SB) or with (SB + U) 8M urea prior to SDS-PAGE with (+) or without (-) boiling and immunoblotted against POTRA or TroA (loading control) antiserum. MW standards (kDA) for SDS-PAGE and immunoblot analyses are on the left of each panel.