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. 2014 Mar 3;111(12):4449–4454. doi: 10.1073/pnas.1323268111

Fig. 4.

Fig. 4.

Probe 4 reveals soluble but nonfunctional TTR in E. coli cell lysate. (A) Structure of folding probe 4. (B and C) Not all soluble WT-TTR and its destabilized A25-TTR mutant in lysate (expressed at similar levels) are functional. Concentrations of total soluble (gray) and soluble folded and functional tetrameric (white) WT-TTR and A25T-TTR in lysate were quantified by (C) quantitative Western blot and (B) probe 4 reactivity, respectively. These concentrations were used to derive the Rf values. Data are represented as mean ± SD. (D) Denatured WT-TTR refolds to predominantly folded and functional TTR tetramer in buffer, whereas folding is 98% prevented by the cellular holdase activity in E. coli lysate created by ATP depletion.