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Chem Commun (Camb) ; 47(28): 8007-9, 2011 Jul 28.
Article in English | MEDLINE | ID: mdl-21670803

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 ß-hairpin Trpzip4 is destabilized by the neat [C(4)mpy][Tf(2)N].


Subject(s)
Ionic Liquids/pharmacology , Peptides/chemistry , Protein Folding/drug effects , Models, Molecular , Protein Structure, Secondary , Pyrroles/pharmacology , Pyrrolidines
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