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. 2014 Dec 12;111(52):18619–18624. doi: 10.1073/pnas.1413994112

Fig. 3.

Fig. 3.

Binding of ssDNA to N-domain shifts the conformational equilibrium. (A) Far-UV CD spectra of the N-domain (1–102) at a protein concentration of 15 µM in the absence (blue) and in the presence of the single-stranded (TG)6 DNA at molar ratio of 1:0.5 (cyan), 1:1 (green), and 1:1.5 (red) (N-domain:DNA). (B) Superimposition of NMR 1H-15N HSQC spectra of the N-domain (1–102) at a protein concentration of 40 µM in the absence (blue) and in the presence of the (TG)6 DNA at molar ratio of 1:1 (red). Purple arrows are used to indicate HSQC peaks from the unfolded form which disappeared in the HSQC spectra in the presence of the (TG)6 DNA at molar ratio of 1:1 (red). (C) The structure of the TDP-43 N-domain in ribbon with residues having HSQC-peak intensity ratios < average value (0.65) colored in green. (D) The electrostatic potential surface of the TDP-43 N-domain structure with the identical orientation as in C and (E) with 180° rotation.