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. 2014 Sep 30;4:6508. doi: 10.1038/srep06508

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Copyright © 2014, Macmillan Publishers Limited. All rights reserved

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(a) Comparison of the folded fraction (f_F) and anisotropy values of Ail-WT (, purple) and the Trp mutants W42F (, blue) and W149F (, grey) refolded in 200 mM LDAO (DPR 7000:1) indicates the presence of a stable intermediate species in the f_F (indicated by an arrow), which is absent in the anisotropy (r) data. Fits are indicated by solid lines that are color-coded to match the corresponding symbols. (b) Plot of the C_m values calculated from the f_F (solid fill) and anisotropy (r) (diagonal stripes) data using linear extrapolation. Color codes are matched to Fig. 3a. For the f_F data, C_m reflects the mid-point of the transition of the ‘adsorbed' protein intermediate to the fully refolded β-barrel form. The lowest C_m is seen in the case of W42F, suggesting destabilization of this protein in very high DPR. Also see Supplementary Figs. 2–4.

Inline graphic — (a) Comparison of the folded fraction (f_F) and anisotropy values of Ail-WT (, purple) and the Trp mutants W42F (, blue) and W149F (, grey) refolded in 200 mM LDAO (DPR 7000:1) indicates the presence of a stable intermediate species in the f_F (indicated by an arrow), which is absent in the anisotropy (r) data. Fits are indicated by solid lines that are color-coded to match the corresponding symbols. (b) Plot of the C_m values calculated from the f_F (solid fill) and anisotropy (r) (diagonal stripes) data using linear extrapolation. Color codes are matched to Fig. 3a. For the f_F data, C_m reflects the mid-point of the transition of the ‘adsorbed' protein intermediate to the fully refolded β-barrel form. The lowest C_m is seen in the case of W42F, suggesting destabilization of this protein in very high DPR. Also see Supplementary Figs. 2–4.