The effects of high concentrations of ionic liquid on GB1 protein structure and dynamics probed by high-resolution magic-angle-spinning NMR spectroscopy |
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Authors: | Lisa Warner Erica Gjersing Shelby E Follett K Wade Elliott Sergei V Dzyuba Krisztina Varga |
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Institution: | 1. National Renewable Energy Laboratory, Golden, CO 80401, USA;2. Department of Chemistry, University of Wyoming, Laramie, WY 82071, USA;3. Department of Chemistry and Biochemistry, Texas Christian University, Fort Worth, TX 76129, USA |
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Abstract: | Ionic liquids have great potential in biological applications and biocatalysis, as some ionic liquids can stabilize proteins and enhance enzyme activity, while others have the opposite effect. However, on the molecular level, probing ionic liquid interactions with proteins, especially in solutions containing high concentrations of ionic liquids, has been challenging. In the present work the 13C, 15N-enriched GB1 model protein was used to demonstrate applicability of high-resolution magic-angle-spinning (HR-MAS) NMR spectroscopy to investigate ionic liquid–protein interactions. Effect of an ionic liquid (1-butyl-3-methylimidazolium bromide, C4-mim]Br) on GB1was studied over a wide range of the ionic liquid concentrations (0.6–3.5 M, which corresponds to 10–60% v/v). Interactions between GB1 and C4-mim]Br were observed from changes in the chemical shifts of the protein backbone as well as the changes in 15N ps-ns dynamics and rotational correlation times. Site-specific interactions between the protein and C4-mim]Br were assigned using 3D methods under HR-MAS conditions. Thus, HR-MAS NMR is a viable tool that could aid in elucidation of molecular mechanisms of ionic liquid–protein interactions. |
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Keywords: | Imidazolium ionic liquid GB1 Ionic liquid–protein interaction HR-MAS NMR |
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