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Fluorescence studies of protein thermostability in ionic liquids
Sheila N Baker1, T Mark McCleskey, Siddharth Pandey
1Chemistry Division, MS J514, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
Chemical Communications (Cambridge, England)
|April 8, 2004
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; T(un) approximately 105 degrees C in [C4mpy][Tf2N] compared to 40 degrees C in bulk water.