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. 2019 Feb 25;9:2650. doi: 10.1038/s41598-018-37072-x

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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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Denaturant effect of MBP unfolding and MBP-maltose binding. (A) T_m of MBP decreases with increasing GdnHCl concentration. (B) MBP-maltose binding with 0.7 M GdnHCl at 35 °C. The value of K_d is 2.3 µM. All the experiments were carried out in triplicate. The protein concentration in all the assays was fixed to 2 µM. All assays were taken in the buffer: 120 mM NaCl, 20 mM NaH₂PO₄/Na₂HPO₄, pH 7.4 with 1% DMSO and the melting program was set to 0.5 °C/min.