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. 2021 Feb 11;11:3551. doi: 10.1038/s41598-021-82893-y

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© The Author(s) 2021

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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Characterization of recombinant F2-P27 protein. (a) Coomassie brilliant blue-stained SDS-PAGE showing purified F2-P27 subunit. Molecular weights (kDa) are indicated on the left margin. (b) Mass spectrometry of recombinant F2-P27 subunit. The mass/charge (m/z) ratios are shown on the x-axes, and the intensities are displayed on the y-axes in arbitrary units (a.u.). (c) Far-UV CD spectra of F2-P27 subunit at different temperatures (35°C, 55°C and 95°C). Mean residue ellipticities (θ) (y-axes) at given wavelengths (x-axes).