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Updated: May 22, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Solvent dependence of helix stability in aromatic oligoamide foldamers
Ting Qi1, Victor Maurizot, Hiroki Noguchi
1Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 2 rue Escarpit, F-33600 Pessac, France. i.huc@iecb.u-bordeaux.fr.
Abstract:
A new helical aromatic oligoamide foldamer, bearing triethyleneglycol side chains for solubility in a broad range of media, was prepared. The stability of the helical conformation was assessed in various solvents and shown to vary greatly and unexpectedly. Stability was remarkably enhanced in methanol-water mixtures.
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