title: 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; T(un) approximately 105 degrees C in [C4mpy][Tf2N] compared to 40 degrees C in bulk water.
authors.affiliation: Chemistry Division, MS J514, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
authors.forename: Sheila N
authors.initials: SN
authors.lastname: Baker
authors.forename: T Mark
authors.initials: TM
authors.lastname: McCleskey
authors.forename: Siddharth
authors.initials: S
authors.lastname: Pandey
authors.forename: Gary A
authors.initials: GA
authors.lastname: Baker
mesh_terms: D018360:Crystallography, X-Ray; D007477:Ions; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012997:Solvents; D013050:Spectrometry, Fluorescence; D013549:Sweetening Agents / Q000737:chemistry; D013696:Temperature; D014364:Tryptophan / Q000032:analysis
chemical_list: D007477:Ions; D010940:Plant Proteins; D011506:Proteins; D012997:Solvents; D013549:Sweetening Agents; C002541:monellin protein, Dioscoreophyllum cumminsii; D014364:Tryptophan