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Issue 32, 2019
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The ionic liquid [C4mpy][Tf2N] induces bound-like structure in the intrinsically disordered protein FlgM

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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

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Article information


Submitted
04 Apr 2019
Accepted
30 Jul 2019
First published
31 Jul 2019

Phys. Chem. Chem. Phys., 2019,21, 17950-17958
Article type
Paper
Author version available

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

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