2015/05/27 by Chevrot, Guillaume, Fileti, Eudes Eterno, Chaban, Vitaly V.
#Biological Physics (physics.bio-ph) #Biomolecules (q-bio.BM) #Chemical Physics (physics.chem-ph) #FOS: Biological sciences #FOS: Physical sciences
paper · doi:10.48550/arxiv.1505.07408
Using molecular dynamics simulations, the structure of model mini-protein was thoroughly characterized in the imidazolium-based amino acid ionic liquids and their aqueous solutions. We report that the mini-protein is more stable when AAIL is added as a cosolvent. Complete substitution of water by organic cations and anions further results in hindered conformational flexibility of the mini-protein. This observation suggests that AAILs are able to defend proteins from thermally induced denaturation. We show by means of radial distributions that the mini-protein is efficiently solvated by both solvents due to agood mutual miscibility. However, amino acid based anions prevail in the first coordination sphere of the mini-protein.