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. 2017 Aug 29;7:9858. doi: 10.1038/s41598-017-07501-4

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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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(a) Scheme of acid-base catalyzed thiol-disulfide exchange reaction proceeding through a classical S_N2 trigonal bipyramidal transition state. (b) Schematic representation of force-clamp MD simulations during which the I27* domain unfolded under constant force application. The five cysteine residues contained in I27* are highlighted (carbon alpha and carbon beta atoms: purple spheres and sulfur atom: yellow sphere). The disulfide bond between 24Cys and 55Cys prevented the protein from fully stretching and stabilized a closed disorder loop. This loop confined two of the three free cysteines (32Cys and 47Cys) in proximity to the 24Cys–55Cys disulfide bond. The third free cysteine, 63Cys, at the C-terminal part of the protein moved away from the disulfide bond upon stretching.