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. 2019 Jun 25;9:9210. doi: 10.1038/s41598-019-45545-w

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© The Author(s) 2019

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Solid state NMR analysis of ¹³C-¹⁵N-labeled CRES amyloids. (a) Structural model for CRES monomer predicted with SWISS MODEL. (b) Chemical shifts for this model were predicted with SHIFTX-2, converted into ¹³C^α-¹³C^β correlation peak lists with FANDAS, and overlaid onto a 2D DARR ¹³C-¹³C correlation spectrum generated from sonicated CRES (gray). The predicted chemical shifts for non-helical sites in the protein agree well with the DARR spectrum (black dots). However, chemical shifts predicted from the α-helix (red) show relatively poor agreement. The agreement between the spectrum and the predicted chemical shifts was improved by converting the secondary structure of the helix into an idealized antiparallel β-hairpin. (c). The movement from the predicted α-helical chemical shifts to the corresponding β-sheet chemical shift for the same site is indicated by the red arrows depicted in (b). The α-helical peak is at the foot, and the predicted β-strand chemical shift is at the head of each arrow. Note that all peaks from the predicted helical region of the protein appear to shift into the strongly-observed β-sheet chemical shift region of the spectrum.