Due Wednesday February 22, 2023 Time required: 70 min. Name: 1. (10 pts, 20min ) CSP (cold shock protein) is produced in bacteria. The wild-type protein contains an lle at position 18 in the chain. You can view the structure of the wild-type and mutant proteins on the Jmol page associated with this problem set. Three different mutant proteins are studied, with the Ile replaced by Ala, Val, or Phe. The thermodynamic parameters for unfolding of the wild-type protein are: H=+200 kJ/mol,S=+600J/mol-deg. The denaturation curves for three of the proteins are shown on the right. The enthalpy and entropy for unfolding for those proteins are given in the table. The fluorescence emission spectra for the Phe mutant at 6 different temperatures is shown below. You can assume the emission wavelength for the fully folded protein is 330nm and for the fully unfolded protein is 360nm. i) Use the fluorescence data for the Phe mutant to obtain the fraction unfolded as a function of temperature. The wavelength for at maximum fluorescence for the 6 temperatures are 331,333.5,339.3,347.5,354.5,357.5nm, respectively. Submit the plot with your problem set (3 pts). ii) Then do a Van't Hoff plot to obtain the enthalpy of denaturation for the Phe protein. Submit your plot with your problem set ( 3 pts). iii) Assuming a Tm=313.6K, determine the entropy of denaturation for the Phe mutant (1 pt). iv) Explain the differences in enthalpy and entropy between the wild-type and all three mutants in terms of the structural differences and the hydrophobic effect ( 3 pts)