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. 2017 Dec 5;7:16994. doi: 10.1038/s41598-017-17259-4

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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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Inner disulfide bond species represents a folding intermediate and displays secondary structure features linked with the native conformation. (A) hCox17 was allowed to re-oxidize after DTT removal at pH 7 (left) and pH 8.4 (right). At defined time points, the reaction was quenched and analyzed by HPLC. (B) RP-HPLC peak areas, from the refolding reaction at pH 8.4, are plotted as function of time. Reduced (solid triangles), intermediate (solid squares) and native (open circles) species. (C) Acid-trapped intermediate I was purified by RP-HPLC, freeze-dried, and dissolved in Tris-HCl (pH 8.4) to reinitiate the folding reaction. Folding reaction was subsequently quenched with acid at different time points and re-analyzed by RP-HPLC. (D) Reduced hCox17 was allowed to air oxidize at pH 8.4 inside a sealed FTIR spectrometer cuvette and the spectra recorded at specific refolding times. The relative contributions of random coil (solid squares) and α-helix (open circles) conformations to the global amide I spectra are plotted as a function of time. (E) Duplicates from the FTIR assay at pH 8.4 were acid-quenched and the different species present in the reaction analyzed by RP-HPLC as indicated above. The area of the reduced specie peak is plotted versus the α-helix content as deduced by FTIR.