Unformatted text preview: compared to 1M.] 4. (24 pts) The protein chymotrypsinogen can exist in two states: a native state (N) characterized as a compact, organized globule, and a denatured state (D) characterized by disorder and randomness. The relative amount of the two states depends on solution conditions such as temperature and pH as described by the following equilibrium: N ↔ D K eq = [D]/[N]. ΔG o = +3.56 kJ/mol based on the equilibrium constant at 327 K. a) Calculate K eq at this temperature (Use R = 0.008314 kJ/mol/ o K). b) From the temperature dependence of K eq , it was determined that ΔH o at 327 K is +0.533 kJ/mol. Calculate ΔS o at this temperature. c) Is the denaturation reaction favorable or unfavorable in terms of the change in enthalpy? Is the denaturation reaction favorable or unfavorable in terms of the change in entropy? d) Is the protein denatured at 327 K?...
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- Fall '11
- pH, buffer solution, sodium phosphate buffer