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. 2019 Feb 26;9:2829. doi: 10.1038/s41598-019-39185-3

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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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Urea-mediated denaturation of WT and single-point mutant DENV2C proteins was monitored by CD. CD spectra were obtained in a Chirascan (Applied Photophysics, United Kingdom) using quartz cuvettes with 0.1-cm path length at 25 °C. The proteins were diluted in 50 mM sodium phosphate buffer (pH 6.0)/200 mM NaCl containing urea concentrations ranging from 0 to 8 M to a final protein concentration of 10 µM. The molar ellipticity at 222 nm was converted into denaturation degree (α) and was plotted against the urea concentration (A). The denaturation degree (α) curves using urea obtained for each protein by CD and tryptophan fluorescence were superimposed and are shown in (B–F).