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Urea at sufficiently high concentration unfolds the secondary structure ofproteins leading to denaturation. In contrast, Choline Chloride (ChCl) andurea, in 1:2 molar ratio form a deep eutectic mixture, a liquid at roomtemperature and protect proteins from denaturation. In order to get amicroscopic picture of this phenomenon, we perform extensive all-atom moleculardynamics simulations on a model protein HP-36. Based on our calculation ofKirkwood-Buff integrals, we analyze the relative accumulation of theseosmolytes around the protein. Additional insights are drawn from the analysesof the translational and rotational dynamics of solvent molecules and also fromthe hydrogen bond auto-correlation functions. In the presence of urea, watershows slow subdiffusive dynamics around the protein backbone as a consequenceof stronger interaction of water molecules with the backbone atoms. Urea alsoshows subdiffusive motion. Addition of choline further slows down the dynamicsof urea restricting its inclusion around the protein backbone. Adding to this,choline molecules in the first solvation shell of the protein shows thestrongest subdiffusive behavior. In other words, ChCl behaves as a nano-crowderby excluding urea from the protein backbone and thereby slowing down thedynamics of the water layer around the protein. This prevents the protein fromdenaturation and makes it structurally rigid which in turn is supported by thesmaller radius of gyration and root mean square deviation values of HP-36 whenChCl is present in the system.

Choline chloride as a nano-crowder protects HP-36 from urea-induced denaturation: Insights from Solvent Dynamics and Protein-Solvent interaction