Figure 4
From: Structure formation during translocon-unassisted co-translational membrane protein folding
Secondary structure contributions over time during GlpG and DsbB cell-free synthesis. Raw SEIRAS spectra of the amide I band during GlpG (left) and DsbB (right) cell-free synthesis, insertion and folding into DMPC nanodiscs. A change in the proportion of each secondary structure type occurs as folding progresses. The black line is the experimental data and the dashed red line is the cumulative fit of the individual Gaussian contributions. Overall GlpG has lower band intensities in comparison to DsbB; this is likely due to the unfavourable insertion of GlpG into DMPC (Fig. 2). Secondary derivative analysis of the raw FT-IR spectra was used to assist in band position assignment (Fig. S3), with all derived band positions provided in Table S2.
