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. 2017 Jul 11;7:5159. doi: 10.1038/s41598-017-05354-5

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© The Author(s) 2017

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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Importance of N-terminal residues. (A) Solubility assay of MbAhpC_41–195 showed low solubility of the protein as reflected in the pellet, labelled as P. SN represents supernatant. (B) MbAhpC_16–195 also showed a less soluble protein (left) and the presence of a laddering pattern (right) in the 125 mM imidazole fraction after affinity chromatography, indicates the presence of undefined oligomers. LM represents a molecular weight standard. Both SDS gels revealed the importance of the N-terminal residues, particularly from residues 1–15, in maintaining the solubility and oligomerization of MbAhpC.