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Creators/Authors contains: "Heyert, Alexanndra J."

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  1. ; ; ; ; (, Physical Chemistry Chemical Physics)
    The A. aeolicus intrinsically disordered protein FlgM has four well-defined α-helices when bound to σ 28 , but in water FlgM loses structure. In this work, we investigate the structure of FlgM in aqueous solutions of the ionic liquid [C 4 mpy][Tf 2 N]. 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 than the bound state. 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. 
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  2. ; ; ; ; ; ; ; ; ; ; et al (, PLOS ONE)
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