Table 3. Apparent thermodynamic parameters for the equilibrium unfolding of RaPrP^C(121–228) and the I214V mutant at 25°C.

Protein	(kJ·mol−1)	(kJ·mol−1·M−1)	(M)
RaPrPC(121–228)	26.2±2.7	−3.88±0.49	6.49±0.05
I214V	16.1±1.8	−2.62±0.38	5.65±0.06

Note: is an estimate of the free energy in the absence of denaturant, the parameter represents the cooperativity of the unfolding transition, and is the concentration of urea at the midpoint of unfolding. The determined parameters for the wild-type [30] are listed here to facilitate comparison.