Figure 2.

The CαCβ and CO region of the ¹³C−¹³C DARR¹¹ spectra for a uniformly ¹⁵N−¹³C-labeled sample of hVDAC2 shown in red contours, and in the presence of erastin in blue contours (hVDAC2e; 750 MHz AVANCE spectrometer with sample spinning at 14 kHz). Dashed lines represent spectral connectivities of ¹³Cα−¹³Cβ and ¹³CO backbone nuclei of residues with strong dependence on secondary structure, alanine (Cα_strand 50.86 ± 1.28 ppm, Cα_helix 54.86 ± 0.94 ppm, Cα_coil 52.67 ± 1.76 ppm and Cβ_strand 21.72 ± 1.77 ppm, Cβ_helix 18.27 ± 1.08 ppm, Cβ_coil 19.03 ± 1.77 ppm), serine (Cα_strand 57.14 ± 1.11 ppm, Cβ_strand 65.39 ± 1.48 ppm), and threonine (Cα_strand 56.28 ± 1.52 ppm, Cβ_strand 70.82 ± 2.11 ppm). Common chemical shifts for backbone carbons for these residues based on the structural environment are given in parentheses.(9)