At low concentrations, thus, [BMIM]⁺ consistently exhibits a higher relative density near the Ubiquitin surface compared to [EMIM]⁺ independently of the accompanying anion. However, this trend shifts with changes in concentration. and ). At low concentrations, thus, the ILs dehydrate the protein and, to a first approximation, act as protein denaturants. However, as the concentration increases, decreases, and the protein becomes preferentially Γ 𝑐𝑝 hydrated, most notably for ILs containing [BMIM]⁺. This would suggest, again in a first approximation, that the ILs would favor the protein folded state at higher concentrations. Note, however, that the aggregate effect of the cosolutes in protein folding depends on the interactions with the denatured states and, as we have shown previously, these ILs interact strongly with Ubiquitin denatured states favoring denaturation at all concentrations.