Fig. 2: 3D structure of the Aβ(1-42) tetramer prepared in DPC.

a Ribbon diagram of the Aβ(1-42) tetramer structure. Aβ(1-42) subunits are colored either red or green to identify the asymmetric dimer unit that constitutes the building block of the Aβ(1-42) tetramer. b Distribution of hydrophobic and charged residues on the surface of the Aβ(1-42) tetramer. Hydrophobic residues are white, polar are yellow, and positively and negatively charged are red and blue, respectively. c Water accessibility of amide protons revealed through 2D [¹H,¹⁵N]-HSQC spectra obtained at different pHs and through measurement of amide temperature coefficients. Solvent accessibility is linearly coded on the basis of the intensity of blue, with light blue corresponding to low water accessibility and dark blue corresponding to high water accessibility. Unassigned residues are shown in gray. d DPC accessibility of amide protons. The residues that showed NOEs between the backbone amide proton and the N-bound methyls of the choline head group of DPC are shown in green. The amide residues that showed paramagnetic enhancement, ε, upon addition of 16-DSA are shown in magenta. The ε values are linearly coded on the basis of the intensity of magenta, with light pink corresponding to ε = 0 and dark magenta corresponding to ε = ε_max. e Solvent Accessible Surface Area (SASA, Ų) from MD simulations of the Aβ(1-42) tetramer in DPC. Detergent micelle is represented as a smoothed transparent surface. The figure was prepared with the program Pymol. Source data are provided as a Source data file.