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. Author manuscript; available in PMC: 2009 Aug 20.

Published in final edited form as: Biochemistry. 2008 Apr 8;47(17):4887–4897. doi: 10.1021/bi702211j

Analysis of the stability of dsRBM1 and dsRBD by equilibrium urea unfolding titrations. Samples were prepared at 0.1 mg/ml (dsRBM1) or 0.15 mg/ml (dsRBD) and incubated at variable urea concentrations at 20°C for 3 hours. CD data were collected at 222 nm in a 5 mm path length cuvette. The data were background-subtracted, normalized and fit with a two-state model (dsRBM1) or a three-state model (dsRBD) using the program SAVUKA. The points are the normalized data for dsRBM1 () and dsRBD (). and the lines are the respective two- and three-state fits. The inset shows the residuals. The best-fit parameters are in Table 1.

Inline graphic — Analysis of the stability of dsRBM1 and dsRBD by equilibrium urea unfolding titrations. Samples were prepared at 0.1 mg/ml (dsRBM1) or 0.15 mg/ml (dsRBD) and incubated at variable urea concentrations at 20°C for 3 hours. CD data were collected at 222 nm in a 5 mm path length cuvette. The data were background-subtracted, normalized and fit with a two-state model (dsRBM1) or a three-state model (dsRBD) using the program SAVUKA. The points are the normalized data for dsRBM1 () and dsRBD (). and the lines are the respective two- and three-state fits. The inset shows the residuals. The best-fit parameters are in Table 1.