. 2001 Oct;10(10):2063–2074. doi: 10.1110/ps.07101

Table 2.

Effects of different mutations on the protein stability of ubiquitin as measured by GdnHCl denaturation

Protein^a	ΔG^H²^O (kcal mol⁻¹)	m value (kcal mol⁻¹M⁻¹)	C_m (M)
wild-type	−5.31 ± 0.46	1.42 ± 0.12	3.74 ± 0.32
E18D	−5.39 ± 0.46	1.51 ± 0.13	3.57 ± 0.30
desG10/E18D	−5.53 ± 0.43	1.58 ± 0.12	3.50 ± 0.27

^a All measurements were performed at room temperature in H₂O with different concentrations of GdnHCl (pH 3). The samples were excited at 277 nm and the tyrosine fluorescence emission was recorded at 303 nm. The free energy changes and m values were obtained by a nonlinear least-squares fit with the fitting errors noted.