Fig. 3: HSQC NMR surface mapping of ionic liquid–protein interactions. | Communications Chemistry

Fig. 3: HSQC NMR surface mapping of ionic liquid–protein interactions.

From: Revealing the complexity of ionic liquid–protein interactions through a multi-technique investigation

Fig. 3

a–c Change in chemical shift for GFP amino acid residues (as measured by 1H-15N HSQC NMR spectroscopy — Supplementary Fig 8) comparing D2O solutions to 1M solutions of [bmim][OAc] (a), [bmim]Cl (b), [bmpyrr][OTf] (c). d–i Corresponding models showing GFP from the side (d, f, h) and from the top (e, g, i) highlighting the shifting amino acids in the presence of [bmim][OAc] (d, e), [bmim]Cl (f, g), [bmpyrr][OTf] (h, i). Residues colored in blue are solvent accessible, and those colored in red are not. The darker colors represent the top ten residues that displayed the greatest shift in chemical shift. Models were created using the PDB ID: 1ema41 with molecular graphics programme, VMD42.

Back to article page