Figure 2.

The BECN1 N-terminal domain is intrinsically disordered. (A) Circular dichroism spectra of BECN1(1–150)[4CS]Y. The mean residue ellipticity ([θ]) is plotted as a function of wavelength. (B) Overlay of ¹H-¹⁵N HSQC spectra of BECN1(1–150)[4CS]Y (black) and BECN1(1-76)[2CS]Y (green) with backbone assignments of BECN1(1–150)[4CS]Y annotated. Resonances corresponding to side-chain NH₂ amides of Asn and Gln are connected by horizontal lines. Resonances arising from the short linker sequence at the N terminus and the extra tyrosine residue added to the C terminus are labeled in red. (C) Secondary structure of BECN1(1–150)[4CS]Y as predicted by CSI 2.0³⁴ based on experimentally observed backbone chemical shifts (¹³C_α, ¹³C_β, ¹³C, ¹⁵N, ¹H_N, and ¹H_α). C: random coil, H: helix. Serine substitutions for native cysteines are indicated in red.