Issue 8, 2004

Fluorescence studies of protein thermostability in ionic liquids

Abstract

Using the single tryptophan residue in the sweet protein monellin as a spectroscopic handle, we show the extreme thermodynamic stabilization offered by an ionic liquid; Tun ∼ 105 °C in [C4mpy][Tf2N] compared to 40 °C in bulk water.

Graphical abstract: Fluorescence studies of protein thermostability in ionic liquids

Supplementary files

Article information

Article type
Communication
Submitted
23 Jan 2004
Accepted
26 Feb 2004
First published
19 Mar 2004

Chem. Commun., 2004, 940-941

Fluorescence studies of protein thermostability in ionic liquids

S. N. Baker, T. M. McCleskey, S. Pandey and G. A. Baker, Chem. Commun., 2004, 940 DOI: 10.1039/B401304M

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