3) [25pts] A particular protein-ligand interaction has H=8kcal/mol and S=12cal/mol.K (measured at 25C, in 10mMNa3PO4 buffer). A. What is the Kd for this interaction? B. If kon is 2105L/ mol.s, calculate half-life for complex dissociation if the preformed complex is immersed into infinite dilution (under these conditions the complex will not reform) (may require you to review your general chemistry notes of unimolecular reactions, such as radioactive decay of an unstable isotope). C. Given that the Kd for this interaction is measured to be 7106mol/L in 200mMNa3PO4 buffer, are the protein and ligand oppositely charged? Why or why not? How does increased ionic strength affect hydrophobic forces? Does increased ionic strength enhance or weaken hydrophobic interactions? Would this effect be reflected in enthalpy or entropy term of the free energy equation