Jump to main content
Jump to site search

Issue 32, 2019
Previous Article Next Article

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

Author affiliations

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.

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 04 Apr 2019, accepted on 30 Jul 2019 and first published on 31 Jul 2019


Article type: Paper
DOI: 10.1039/C9CP01882D
Phys. Chem. Chem. Phys., 2019,21, 17950-17958

  •   Request permissions

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

    E. E. Carter, A. J. Heyert, M. De Souza, J. L. Baker and G. E. Lindberg, Phys. Chem. Chem. Phys., 2019, 21, 17950
    DOI: 10.1039/C9CP01882D

Search articles by author

Spotlight

Advertisements