Figure EV1. Related to Figs 1 and 2. NMR spectra of Bax (α2–α5) in bicelles and solution with assignments.

• A
  2D ¹H–¹⁵N TROSY‐HSQC spectrum of the uniformly [¹⁵N, ¹³C, ²H]‐labeled Bax (α2–α5) protein in DMPC/DHPC bicelles (q = 0.5) recorded at ¹H frequency of 600 MHz. The backbone amide resonances were assigned to the indicated residues.
• B
  2D ¹H–¹⁵N TROSY‐HSQC spectrum of the uniformly [¹⁵N, ¹³C, ²H]‐labeled soluble Bax (α2–α5) protein recorded at ¹H frequency of 600 MHz. The backbone amide resonances were assigned to the indicated residues.
• C
  NMR chemical shift changes of Bax (α2–α5) upon the addition of the bicelles. The plot of chemical shift changes between the spectra of bicelle‐bound Bax (α2–α5) and soluble Bax (α2–α5). The combined chemical shift changes (Δδ) were calculated by using the equation: $\mathrm{\Delta }\mathrm{\delta }=\sqrt{{\left({\omega }_H\mathrm{\Delta }{\delta }_H\right)}^2+{\left({\omega }_N\mathrm{\Delta }{\delta }_N\right)}^2}$ where ∆δ_H and ∆δ_N are chemical shift changes (in ppm) in the ¹H and ¹⁵N dimensions, respectively, and ω _H and ω _N are normalization factors (ω _H = 1.00, ω _N = 0.15).
• D
  The chemical shift changes of Bax (α2–α5) were mapped to the structure of the bicelle‐bound Bax (α2–α5), colored in one chain according to the scale of chemical shift changes shown below.

Source data are available online for this figure.