Fig. 2 | Nature Communications

Fig. 2

From: Energy landscape underlying spontaneous insertion and folding of an alpha-helical transmembrane protein into a bilayer

Fig. 2

Structural mechanism of the rate-limiting step of refolding at low force. Progression of folding is shown from top to bottom. The structure labels (I1, α, β, γ, and TS) are the same as those used in Fig. 1. The structure of GlpG is colored according to sequence index from red (N-terminal, TM1) to blue (C-terminal, TM6). TM1 is red, TM2 is yellow, TM3 is yellow-green, TM4 is green, TM5 is light blue, and TM6 is dark blue. For each state, several representative structures are aligned and overlayed. Translucent panels are shown to indicate the locations of the upper and lower bilayer interfaces. In I1, TM5–6 are on the bilayer interface. As folding proceeds, TM5 and then TM6 are pulled into the bilayer and fold onto TM1–4

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