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Issue 30, 2014
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Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins

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Abstract

Significant non-reversible two-state denaturation was observed for proteins such as myoglobin (Mb) and α-chymotrypsin (CT) with decreasing temperature in the presence of 1-butyl-3-methylimidazolium-based ([C4mim]+X) ionic liquids (ILs) with various anions (X). Interestingly, for the first time, ILs having acetate and bromide anions were proven to counteract the cold-induced unfolding of proteins.

Graphical abstract: Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins

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Publication details

The article was received on 08 Mar 2014, accepted on 16 May 2014 and first published on 19 May 2014


Article type: Communication
DOI: 10.1039/C4CP01001A
Citation: Phys. Chem. Chem. Phys., 2014,16, 15806-15810
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    Quantitative evaluation of the ability of ionic liquids to offset the cold-induced unfolding of proteins

    A. Kumar, A. Rani, P. Venkatesu and A. Kumar, Phys. Chem. Chem. Phys., 2014, 16, 15806
    DOI: 10.1039/C4CP01001A

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