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. 2017 Nov 2;8:1273. doi: 10.1038/s41467-017-01249-1

Fig. 3.

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)