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Using molecular dynamics simulations, the structure of model mini-protein wasthoroughly characterized in the imidazolium-based amino acid ionic liquids andtheir aqueous solutions. We report that the mini-protein is more stable whenAAIL is added as a cosolvent. Complete substitution of water by organic cationsand anions further results in hindered conformational flexibility of themini-protein. This observation suggests that AAILs are able to defend proteinsfrom thermally induced denaturation. We show by means of radial distributionsthat the mini-protein is efficiently solvated by both solvents due to agoodmutual miscibility. However, amino acid based anions prevail in the firstcoordination sphere of the mini-protein.

Enhanced Stability of the Model Mini-protein in Amino Acid Ionic Liquids and Their Aqueous Solutions