1. For a protein, P, which has a hyperbolic binding curve for a ligand, L, (like a michaelis menten enzyme) choose a dissociation constant in the nano- or micromolar range. Choose a series of ligand concentrations, and plot the fraction of sites occupied on the Y axis against the ligand concentration on X. Be sure the ligand concentrations are chosen so that all or nearly all the binding curve is shown in your plot.
2. For a protein P which has an allosteric binding curve for a ligang L choose a dissociation constant in the nano- or micromolar range as well as a hill coefficient. Choose a series of ligand concentrations, plot the fraction of sites occupied on the Y axis against the ligand cocntrations are chosen so that all or nearly all the binding curve is shown in your plot.
(b) In addition to the plot requested in a above for the allosteric protein, prepare a hill plot
(c) Make a hill plot for the data in exercise 1 above. plot the hill data on the same graph as for (b) above. How do the two plots differ?