Skip to main content
. Author manuscript; available in PMC: 2021 Jul 24.
Published in final edited form as: J Mol Biol. 2020 May 26;432(16):4388–4407. doi: 10.1016/j.jmb.2020.05.018

Figure 3.

Figure 3.

A) Secondary structure of peptide residues in the 150 kDa Aβ(1–42) oligomer, predicted by TALOS-N software, and the measured secondary 13C NMR backbone chemical shifts upon which the TALOS-N prediction is based. B) The NMR linewidths of CO (green), Cα (red), and Cβ (blue) reported as full widths at half maximum measured by nonlinear regression of cross peaks in the 2D-fpRFDR 13C-13C NMR spectra to Gaussian functions.