4.7 Article

Fluorescence studies of protein thermostability in ionic liquids

Journal

CHEMICAL COMMUNICATIONS
Volume -, Issue 8, Pages 940-941

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/b401304m

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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-u similar to105 degreesC in [C(4)mpy][Tf2N] compared to 40 degreesC in bulk water.

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