. 2013 Jun 24;110(28):11337–11342. doi: 10.1073/pnas.1222245110

Table 1.

Thermodynamic parameters for the unfolding of WT HP36 and the mutants

Protein	T_m, °C	ΔH°(T_m), kcal⋅mol⁻¹	ΔG°, kcal⋅mol⁻¹	m-value	C_M^*, M
WT HP36	73.0 ± 0.2	31.82 ± 0.33	3.17 ± 0.06	0.52 ± 0.01	6.2
K48M	78.0 ± 0.4	34.07 ± 0.38	4.11 ± 0.08^†	0.52 ± 0.01^‡	7.9
K65M	77.2 ± 0.6	33.20 ± 0.65	3.87 ± 0.08^†	0.52 ± 0.01^‡	7.2
K70M	82.2 ± 0.7	33.44 ± 0.44	4.37 ± 0.08^†	0.52 ± 0.01^‡	8.4

Experiments were conducted in 10 mM sodium acetate, 150 mM sodium chloride at pH 5.0. SEs of the fit are provided as measures of parameter uncertainty.

The C_M value was determined by calculating the derivative of the plot of CD signal vs. [urea].

^{^†}

The ΔG° values are calculated using the following: ΔG° = C_M × m value.

^{^‡}

The high thermal stability of the variants prevents an accurate determination of the m-value (given in kilocalories per mole-molarity), so the value of WT HP36 is used.