title: The effect of neat ionic liquid on the folding of short peptides.
abstract: 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].
authors.affiliation: Department of Chemistry, The College of New Jersey, 2000 Pennington Rd., Ewing, NJ 08628, USA.
authors.forename: Jia Lin
authors.initials: JL
authors.lastname: Huang
authors.forename: Michael E
authors.initials: ME
authors.lastname: Noss
authors.forename: Karson M
authors.initials: KM
authors.lastname: Schmidt
authors.forename: Leigh
authors.initials: L
authors.lastname: Murray
authors.forename: Michelle R
authors.initials: MR
authors.lastname: Bunagan
mesh_terms: D052578:Ionic Liquids / Q000494:pharmacology*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding / Q000187:drug effects*; D017433:Protein Structure, Secondary; D011758:Pyrroles / Q000494:pharmacology; D011759:Pyrrolidines
chemical_list: C521242:1-butyl-1-methylpyrrolidinium bis(trifluoromethylsulfonyl)amide; D052578:Ionic Liquids; D010455:Peptides; D011758:Pyrroles; D011759:Pyrrolidines