Native PAGE profiles of BSX and R-BSX.

<p>(A) and (B) show native-PAGE profiles of thermal unfolding of proteins at room temperature and at 60°C, respectively. V1G was found to unfold after incubation at 60°C for 15 min, whereas no significant unfolding was observed for all the other mutants. Note the slightly faster mobility of R-BSX when compared to BSX, reconfirming the results obtained in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0003063#pone-0003063-g002" target="_blank">Figure 2C</a>. (C) and (D) show SDS-PAGE profiles of all the proteins in the absence and presence of proteinase K, respectively. Note that all proteins except V1G and BSA (indicated by arrow) showed proteinase K resistance.