Fig. 1: The N-terminal domains of D10 and D2 are disordered in solution.
From: Amyloid fibril structures link CHCHD10 and CHCHD2 to neurodegeneration
a Schematic of full-length human CHCHD10 and CHCHD2 delineating the putative mitochondrial targeting sequence (MTS, red), central α-helix domain (green), and the coiled-coil-helix-coiled-coil-helix (CHCH) domain (blue). The N-terminal (NT) fragments used in this study are indicated. b CD spectra of WT D10-NT (black) and WT D2-NT (green). c, d NMR 15N-1H HSQC spectra of WT D10-NT (c) and WT D2-NT (d) annotated with backbone resonance assignments (see Supplementary Figs. 15 and 16 for full-page versions). e, f Secondary carbon chemical shifts of WT D10-NT (e) and WT D2-NT (f). g, h Graphical representation of secondary structure determined by CheSPI for WT D10-NT (g) and WT D2-NT (h). The horizontal grey bar indicates a random coil (no secondary structure). The magenta sinusoidal line for D10-NT indicates the presence of one turn of a 3–10 helix for the final three C-terminal residues. Source data for b, e, and f are provided as a Source Data file.
