Electrostatic interactions in hemoglobin from light scattering experiments

Light scattering experiments on solutions of bovine CO-hemoglobin have revealed that a substantial component of the interactions responsible for the protein stability versus tetramer-to-dimer dissociation is due to electrostatic effects. Their magnitude has been estimated to reach ≃4 kcal/mole (≃0.15 eV) at pH=5 compared with the nonelectrostatic term which is of the order of 7 kcal/mole (≃0.3 eV).