Suppose you have a protein whose natively folded state is more stable than the unfolded state by 20 kJ/mol (i. e. ΔG0 for folding is ‐20 kJ/mol) in the absence of denaturant. Suppose that the stability of the protein decreases (i. e. ΔG0 increases) in proportion to the concentration of denaturant, by 10 kJ/mol per 1 molar concentration of denaturant. b) Now suppose that the fluorescence of the folded protein is 400 (in arbitrary units) and 250 for the unfolded protein. Write a computer program (e. g. in the iPython notebook system) to calculate and plot what the fluorescence of the protein sample would look like as a function of the concentration of the denaturant. [Hint: You will probably want to set up arrays for the denaturant concentration and the fluorescent readout, and then write a loop that changes the denaturant concentration and calculates the new fluorescence value, and stores those two values in their respective arrays.]

denat_save=[ ]

fluor_save=[ ]

for i in range (100):

denat=i/10. #this will sample concentrations from 0 to 10M

denat_save. append(denat)

#Now calculate the value of delta G0 at this denaturant concentration

#Then calculate the fractions of the folded and unfolded states

#Then calculate the expected fluorescent value, and store this

#value in the array fluor_save

#When your loop contains the necessary calculations, leave

#the loop by unindenting. Then plot the result by sending the

#two arrays (denat_save and fluor_save) to the plotting program.

plt. plot(denat_save, fluor_save)