Ionic liquids (ILs) in aqueous solution can affect the structure and stability of proteins. Since ILs can affect helices and sheets differently it is an open question how they affect mixed-structure proteins. In this presentation the effects of ILs on the stabilities of the mixed-structure proteins azurin and nitrite reductase were investigated using thermal and surfactant-based unfolding. Protein unfolding was monitored using either infrared or fluorescence spectroscopy. The ILs included both imidazolium chloride and novel amino acid-based ILs. The results provide unfolding enthalpy and entropy values as well as structural insight into how different protein domains unfold in the presence of the ILs.

Unfolding of mixed-structure proteins in the presence of ionic liquids in aqueous solutions

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.