C. Borges, Júlio V. Seraphim, Thiago Z. Mokry, David C. L. Almeida, Fabio M. Cyr, Douglas H. I. Ramos, Carlos Thermal-induced unfolding measurements followed by DSC. <p>(<b>A</b>) Sis1; (<b>B</b>) Sis1_Δ<sub>124–174</sub>; (<b>C</b>) Sis1_Δ<sub>121–257</sub> and (<b>D</b>) SYS. The figures represent the first and second scans after baseline treatment. Sis1 and Sis1_Δ<sub>124–174</sub> showed two overlapping transitions with similar <i>Tm</i>s of approximately 59 and 67°C (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050927#pone-0050927-t001" target="_blank">Table 1</a>). Sis1_Δ<sub>121–257</sub> and SYS showed two well separated unfolding transitions where the second Tm was within 64–66°C (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050927#pone-0050927-t001" target="_blank">Table 1</a>). For all proteins, the second unfolding transition was more than 95% reversible. The first unfolding transition of Sis1, Sis1_Δ<sub>124–174</sub> and Sis1_Δ<sub>121–257</sub> was approximately 90% reversible when the proteins were heated to 90°C. SYS (Fig. D) presented a reversibility of approximately 60% when heated to 90°C. However, when SYS was heated to 50°C (Fig. <b>D</b>, inset) it was more than 95% reversible. Similar behaviors were observed with other proteins. <b>E–F)</b> Kirchoff plots showing the dependence of <i>ΔH</i><sup>cal</sup> with <i>Tm</i> for <i>Sis1</i> and its mutants. Urea concentrations from 0.25 M to 2.0 M were used in order to disturb both <i>ΔH</i><sup>Cal</sup> and <i>Tm</i> that were monitored by DSC. The figure shows the Kirchoff plot for the first (<b>E</b>) and second (<b>F</b>) thermal-induced unfolding transition. The curves were fitted using Eq. 3 in order to obtain the <i>ΔCp</i> for each unfolding transition.</p> unfolding;followed 2013-02-19
    https://plos.figshare.com/articles/figure/_Thermal_induced_unfolding_measurements_followed_by_DSC_/201929
10.1371/journal.pone.0050927.g005