Table 1. Thermodynamic unfolding parameters measured by equilibrium GdnCl denaturation.
The parameters ΔG°u (Gibbs free energy of unfolding in the absence of denaturant), m (cooperativity of unfolding), and Cm (midpoint concentration of denaturant required to unfold 50% of the protein) were determined by GdnCl denaturation and from the integration of the fluorescence intensity. The differences in Cm and ΔG°u values in comparison to the free enzyme are also shown (ΔCm and ΔΔG°u respectively). cvRTPase, chlorella virus RNA triphosphatase.
| Protein | Cm (M) | ΔCm (M) | m (kJ·mol−1·M−1) | ΔG°u (kJ·mol−1) | ΔΔG°u (kJ·mol−1) |
|---|---|---|---|---|---|
| cvRTPase | 1.15 | 0.00 | 3.89 | 7.11 | 0.00 |
| cvRTPase· | 0.55 | −0.60 | 3.84 | 4.28 | −2.83 |
| decavanadate | |||||
| cvRTPase·ATP | 0.80 | −0.35 | 6.66 | 6.42 | −0.69 |
| cvRTPase·ATP· | 0.50 | −0.65 | 1.41 | 3.46 | −3.65 |
| decavanadate |