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. 2019 Mar 7;9:3787. doi: 10.1038/s41598-019-40516-7

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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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Impact of given amino acid substitutions on the oligomeric state of CaiT in detergent solution. (a) BN-PAGE of wild-type and given CaiT variants. Respective genes were expressed in E. coli, and the proteins were purified by Ni-NTA affinity chromatography as described¹. The resulting protein (5 µg per lane) was subjected to BN-PAGE following established protocols^12,40. Proteins were separated using a 4–16.5% gradient gel. The HMW Native Marker Kit (Amersham Biosciences) was used for molecular weight estimation. (b) Gel filtration profile of wild-type and CaiT variants. Proteins (100 µg of each variant solubilized in 0.04% DDM) were analyzed individually with a Superdex 200 10/300 GL column (GE Healthcare). Protein was detected by absorbance measurement at 280 nm.