Protein denaturations are usually irreversible but may be reversible under a narrow range of conditions. At pH 2.0, at temperatures ranging from about 40 degrees celcius to 50 degrees celcius, there is an equilibrium between the active form P and the deactivated form D of the enzyme trypsin: P --> D

Question

Protein denaturations are usually irreversible but may be reversible under a narrow range of conditions. At pH 2.0, at temperatures ranging from about 40 degrees celcius to 50 degrees celcius, there is an equilibrium between the active form P and the deactivated form D of the enzyme trypsin: P --> D

Thermodynamic values are Stardard Delta H = 283 kJ/mol and Stardard Delta S = 891 J/Kmol. Assume these values to be temperature independent over this narrow range. At what temperature will there be equal concentrations of P and D?

Answer 1

given the Joule-thompson coefficient and change is pressure and the initial temperature how do you find temperature of liberated gas