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Ionic liquids (ILs) are considered as green solvents, and some ILs can stabilize proteins. ILs find significant importance from the perspectives of protein-ionic liquid (P-IL) interactions. An arsenal of nuclear magnetic resonance (NMR) methodologies can be employed to probe the differential binding and dynamics of cation and anion of ILs with the proteins of interest towards targeted functionalities. This chapter focusses on the recent developments of NMR spectroscopy on binding and dynamics of ILs as well as proteins, with a view to appreciate P-IL interactions. The favourable outcome of P-IL interactions can be exploited by employing various NMR approaches such as 1H lineshapes, chemical shifts, spin-spin and spin-lattice relaxation (both selective and nonselective), translational self-diffusion, saturation transfer difference (STD), 1H-15N heteronuclear single-quantum correlation (HSQC) and High-resolution magic angle spinning (HRMAS). These experiments facilitate the extraction of fruitful information on mobility, size and spatial proximities, and preferential binding sites of ion species as well as proteins. In this scenario, we highlight here some of the recent NMR advances and future research directions in this important area. |
