Mechanism of Stabilization of Helical Conformations of Polypeptides by Water Containing Trifluoroethanol
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文摘
For conjugates Ac-Hel1-Alan-OH,n = 1-6, of the previously characterized reporting,conformationaltemplate Ac-Hel1, increases in helicity induced bytrifluoroethanol (TFE) in water have been related to asimplefunction of the peptide length n, yielding the helixpropagation constant sAla, which increases from1.0 to 1.5 forfchars/chi.gif" BORDER=0 >TFE = 0-20 mol %. The per-residue helicityincrease is similar to the increase in te state stability induced byTFEin monoamide conjugates Ac-Hel1-NHR. Addition of TFEto water significantly increases the rate ofinterconversionof s-cis/s-trans amide conformers for Ac-Pro-NHMe, consistent with asignificant and selective destabilization ofthe planar resonance-stabilized amide. In dilute aqueous solutionTFE increases helicity by selectively destabilizingamide functions that are solvent exposed, with the consequence thatcompact conformations such as helices thatmaximize intramolecular amide-amide hydrogen bonding and minimizeamide solvent exposure are selectivelyfavored.

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