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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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Influence of secondary structure in the oxidative folding of hCox17. (A) Far-UV CD spectra of reduced hCox17 in the absence (upper solid line) and in the presence of 10% (dashed line), 20% (dotted line) and 40% (lower solid line) of TFE. The characteristic α-helix 222 nm signal is indicated as a vertical dotted line. (B) Reduced hCox17 was allowed to refold in the presence of increasing concentrations of TFE. After 1 h of reaction, the samples were acid-quenched and analyzed by RP-HPLC. The native peak area was integrated and plotted as a function of TFE concentration. (C) Reduced hCox17 mutant H1 (circles), H2 (squares) and wild type (solid triangles) proteins were allowed to refold and the normalized native RP-HPLC peak areas are plotted as a function of the refolding time. (D) hCox17 refolding in the presence of increasing concentrations of Guanidine-HCl was quenched with TFA after 2 hours of reaction. The amount of native (solid triangles), intermediate (solid squares) and reduced (open circles) species are plotted as a function of denaturant concentration.