The fact that titration curves of peptides rotate as ionic strenght increases, is evidence of electrostatic interaction at colloidal dimensions between discrete molecules? As ionic strenght begins to increrase, longer ranged electrostatic saline bonds are diminished by the Debye-Hückel shielding. This is the nature of salting-in of peptides. Salting-out at higher ionic strenghts is due to the diminution of the zwitterion conformer because of increased cannonical (uncharged tautomer form) Any comments?