Figure 3.

(a) turbidity of complexes of BLG with pectin with varying pH at different NaCl concentrations, where pH_ϕ1 and pH_ϕ2 denote pH at aggregation and dissolution of complexes. Reprinted with permission from Ref. [91]. Copyright 2007, American Chemical Society. (b) turbidity of BSA-PDADMAC as a function of pH at 50 mM salt, where pH_C denotes pH at which soluble complexes begin to form. Reprinted with permission from Ref. [92] Copyright 2010, American Chemical Society; (c) binding constants of BLG-NaPSS and BLG-PAMPS as a function of salt concentration: (Filled diamond) BLG-NaPSS at pH 7.0; (Filled square) BLG-NaPSS at pH 6.7; (Filled triangle) BLG-NaPSS at pH 6.3; (Open inverted triangle) BLG-PAMPS at pH 6.3; (Open Circle) BLG-PAMPS at pH 6.1; (Addition symbol) BLG-PAMPS at pH 6.1. Reprinted with permission from Ref. [76] Copyright 2003, American Chemical Society; (d) schematic for supercharging of proteins by succinic anhydride; (e) the expected charge on modified proteins with varying degrees of supercharging; (f) change in turbidity as a function of ratio of negative to positive charge residues on proteins. Grey area depicts complexes which do not phase separate; (d), (e) and (f) are reproduced from Ref. [93] with permission from the Royal Society of Chemistry.