Table 3. Thermodynamic unfolding parameters measured by thermal denaturation.
The thermodynamic parameters of unfolding ΔHVH (van't Hoff enthalpy of denaturation) and ΔS (entropy of denaturation) were determined by thermal denaturation of the unliganded cytomegalovirus DNA polymerase and the protein bound to various ligands. Temperatureinduced denaturations were monitored by CD spectroscopy at 222 nm. 1 kcal=4.184 kJ.
Protein | Tm (°C) | ΔHVH (kcal/mol) | ΔS (kcal·mol−1·K−1) |
---|---|---|---|
UL54 | 56.2 | −82.0 | −0.25 |
UL54·DNA | 56.8 | −56.4 | −0.17 |
UL54·DNA·dATPαS·Mg2+ | 54.6 | −86.3 | −0.26 |