Fig. 3.
Isothermal titration calorimetry (ITC) shows that sequence effects in coacervation are entropically driven. a The enthalpic contribution to coacervation as a function of τ is small, positive, and does not show significant differences between sequences. Isothermal titration calorimatry captures this thermodynamic value via a fit to an established two-step coacervation model (inset) that distinguishes between enthalpic contributions from ion pairing (IP) and coacervation (Coac) steps48. b The entropic contribution to the coacervation free energy is large, negative, and attributed to counterion release. Clear differences are observed as a function of τ, with an increasing entropic driving force with increasing blockiness (larger τ)