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. 2017 Sep 29;7:12471. doi: 10.1038/s41598-017-12748-y

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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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Suppression of irreversible denaturation of disulphide bond-containing small globular proteins by MTS reagents. Effects of TAPS-sulfonate (A) and MMTS (B) on the irreversible denaturation of HEL upon heating at 100 °C. (C) Effect of MTS reagents on the irreversible denaturation of RNase A upon heating at 90 °C. (D) Comparison of reversed-phase HPLC elution profiles for native and heated samples of HEL (20 µg). Elution times for denatured and fully formed alkyl disulphide derivatives of HEL are indicated by arrows. (E) Effects of thiol reactive reagents on irreversible denaturation of HEL and RNase A upon heating at 100 °C. N.D., not detectable. SDS-PAGE analysis of HEL (F) and RNase A (G). All heating experiments were performed in HEPES buffer, pH 6.8. Error bars indicate the standard deviation.