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. 2024 Mar 29;15:2750. doi: 10.1038/s41467-024-46832-5

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 7 — a 1D ¹³C cross polarization spectra show the rigid fibril cores of LBD1 (blue), LBD6 (red) and LBD7 (black) amplified fibrils. The aliphatic region of the spectra is shown, highlighting the similarities in the peak positions and relative intensities between the samples. b, c 2D ¹³C-¹³C correlation spectra with 1 ms POSTC7 mixing of (b) LBD6 and (c) LBD1 fibrils. Black contours (positive) correspond to correlations between bound ¹³C nuclei pairs, and red contours (negative) correspond to correlations of ¹³C nuclei two atoms apart. The chemical shifts are highly similar overall, in particular for diagnostic sidechains of Ala, Thr and Val residues.