Fluorescence studies of protein thermostability in ionic liquidsElectronic supplementary information (ESI) available: synthesis of [C4mpy][Tf2N]. See http://www.rsc.org/suppdata/cc/b4/b401304m/
- 19 March 2004
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Communications
- No. 8,p. 940-941
- https://doi.org/10.1039/b401304m
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.Keywords
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