ILs can interact with proteins through hydrogen bonds, established typically by the anions, coulombic interactions with charged residues, and dispersive-like interactions . ILs cations, typically of greater hydrophobic character, might alter the chemical environment surrounding the proteins, by establishing dispersive-like interactions with residues in the protein surface . The surrounding chemical environment of the protein can also be perturbed by anions breaking the hydrogen bonds between the protein and water . In parallel, a known stabilization effect of ILs on protein stability comes from the increased viscosity of the solutions, which slows down the protein motions. The viscosity can also be tuned by increasing the size of the ions .