Fig. 6: Binding of hAtg3∆90-190_P21A to bicelles induces structural changes different from the wild-type protein. | Nature Communications

Fig. 6: Binding of hAtg3∆90-190_P21A to bicelles induces structural changes different from the wild-type protein.

From: An N-terminal conserved region in human Atg3 couples membrane curvature sensitivity to conjugase activity during autophagy

Fig. 6

a, b Overlay of TROSY spectra of 2H,15N,13C-labeled hAtg3∆90-190 (blue) and hAtg3∆90-190_P21A (red) in aqueous solution (pH 7.5) and in bicelles (DMPC:DMPG:DHPC = 4:1:20, molar ratio, pH 7.5), respectively. Both spectra were acquired on a Bruker 600 MHz spectrometer at 25 °C. c and d Plots of chemical shift differences (∆δ) between hAtg3∆90-190 and hAtg3∆90-190_P21A against residue numbers in aqueous solution and in bicelles, respectively.

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