Fluorescence studies of protein thermostability in ionic liquids.
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.
Baker
Sheila N
SN
Chemistry Division, MS J514, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
McCleskey
T Mark
TM
Pandey
Siddharth
S
Baker
Gary A
GA
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
D007477:Ions; D010940:Plant Proteins; D011506:Proteins; D012997:Solvents; D013549:Sweetening Agents; C002541:monellin protein, Dioscoreophyllum cumminsii; D014364:Tryptophan