The ionic liquid [C4mpy][Tf2N] induces bound-like structure in the intrinsically disordered protein FlgM

Erin E. Carter, Alexanndra J. Heyert, Mattheus De Souza, Joseph L. Baker, Gerrick E. Lindberg

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The A. aeolicus intrinsically disordered protein FlgM has four well-defined α-helices when bound to σ28, but in water FlgM undergoes a change in tertiary structure. In this work, we investigate the structure of FlgM in aqueous solutions of the ionic liquid [C4mpy][Tf2N]. We find that FlgM is induced to fold by the addition of the ionic liquid, achieving average α-helicity values similar to the bound state. Analysis of secondary structure reveals significant similarity with the bound state, but the tertiary structure is found to be more compact. Interestingly, the ionic liquid is not homogeneously dispersed in the water, but instead aggregates near the protein. Separate simulations of aqueous ionic liquid do not show ion clustering, which suggests that FlgM stabilizes ionic liquid aggregation.

Original languageEnglish (US)
Pages (from-to)17950-17958
Number of pages9
JournalPhysical Chemistry Chemical Physics
Volume21
Issue number32
DOIs
StatePublished - 2019

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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