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).
No takes yet. Share an insight, caveat, or question.
Lunelli et al. (1993) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: