The Effects of High Concentrations of Ionic Liquid on GB1 Protein Structure and Dynamics Probed by High-Resolution Magic-Angle-Spinning NMR Spectroscopy

Erica Gjersing, Lisa Warner, Shelby Follett, K. Elliott, Sergei Dzyuba, Krisztina Varga

Research output: Contribution to journalArticlepeer-review

22 Scopus Citations

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.
Original languageAmerican English
Pages (from-to)75-80
Number of pages6
JournalBiochemistry and Biophysics Reports
Volume8
DOIs
StatePublished - 2016

NREL Publication Number

  • NREL/JA-5100-68988

Keywords

  • GB1
  • HR-MAS NMR
  • imidazolium ionic liquid
  • ionic liquid-protein interaction

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