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. 2020 Jan 31;10:1570. doi: 10.1038/s41598-020-57775-4

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© The Author(s) 2020

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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Measured CD spectra of apoMb in different folding states. The curve of apoMb at pD 6 has the typical profile of a globular protein with a significant content of helical structure. The curves of apoMb at pD 2 and in 3 M GdmCl are typical random coils, unfolded states. The spectrum of pD 4 validates the partially folded state of apoMb.