Biopolymers as well as functional synthetic polymers in solution are subject to a complex set of interactions that are decisive for their molecular structure and function, e.g., as for folded versus unfolded states for proteins, or, more general, collapsed versus swollen states of a polymer. Typically those solvated polymers are weakly charged and constitute relatively heterogeneous, partially polar, partially hydrophobic, macromolecules. Hence their polymeric structure is greatly affected by the solvation environment. Apart from the solvent type (e.g., water), the polymer conformation can be conveniently controlled by the concentration and type of added cosolutes. In particular, ion-specific, also called Hofmeister effects 2,3 of salts on biopolymeric structure and phase behavior have been studied and highlighted in the recent years in an overwhelming amount of literature. The Hofmeister effects on the polymeric structure and the phase behavior are very complex and polymer specific. In order to increase the accessibility to the problem, often model systems are employed. For instance, the poly-N-isopropylacrylamide (PNIPAM) homopolymer or elastin-like polypeptides (ELPs), which both exhibit hydrophobic collapse transitions at their respective lower critical solution temperatures (LCST). These collapse transitions are analogous to cold-denaturation of proteins, in which ion-specific interactions (Hofmeister effects) play an prominent role.