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. 2009 Mar 24;10(3):1369–1385. doi: 10.3390/ijms10031369

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© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 3. — GdnHCl-induced unfolding (blue circles) and refolding (red circles) curves of Tk-RNase HII at (a) 50 °C for two weeks and (b) 20 °C for one month, monitored by measuring CD at 220nm. The solid line in (a) is the best fit to a two-state equation. For unfolding, Tk-RNase HII was incubated in GdnHCl at different concentrations. For refolding, the protein, which was unfolded completely at a 4M GdnHCl concentration, was diluted with buffer and the diluted protein solution was incubated. Figures are reproduced from [20].