Chemical Communications · 2011 · 37 citations · 12 references
Unusual Folding BehaviourBiochemistryNeat Ionic LiquidProtein FoldingNatural SciencesPeptide Engineeringβ-Hairpin Trpzip4Conformational StudyPeptide SynthesisShort PeptidesPeptide ScienceMolecular BiophysicsChemistryProtein RefoldingMedicineDeep Eutectic SolventBiophysics
Using circular dichroism spectroscopy, we show evidence of unusual folding behaviour for several designed peptides in neat ionic liquid. Helical peptides, AKA(2) and Trp-cage, exhibit heat-induced folding, with stable helical structure persisting to 96 °C, whereas the β-hairpin Trpzip4 is destabilized by the neat [C(4)mpy][Tf(2)N].
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Sheila N. Baker, T. Mark McCleskey, Siddharth Pandey et al. · Chemical Communications · 2004 · 231 citations