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In the case of AAAs 4 and 5 it is imperative to avoid prolonged existence of the intermediate iminophosphorane by using anhydrous reaction conditions. In anhydrous THF, the intermediate iminophosphorane suffered from nucleofilic attack of the iminophosphorane nitrogen on the AAA carbonyl, resulting in loss of the AAA moiety as depicted below. Premixing the THF with H2O prevented this side reaction to occur as gauged by LCMS analysis See the proposed side reaction during Staudinger reduction
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2O prevented this side reaction to occur as gauged by LCMS analysis (See the proposed side reaction during Staudinger reduction.)
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The position of the Hα resonance signal of a residue in a particular peptide, relative to the value of that same residue in a random coil configuration (the chemical shift perturbation, Δ δHα) can be used as an indication of the configuration of that residue. A value of ΔδHα > 0.1 ppm indicates a β-strand, -0.1 < ΔδHα < 0.1 indicates a rondam coil and Δδ Hα < -0.1 ppm indicates a helical configuration. D. S. Wishart, B. D. Sykes, F. M. Richards, Biochemistry 1992, 31, 1647-1651.
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The position of the Hα resonance signal of a residue in a particular peptide, relative to the value of that same residue in a random coil configuration (the chemical shift perturbation, Δ δHα) can be used as an indication of the configuration of that residue. A value of ΔδHα > 0.1 ppm indicates a β-strand, -0.1 < ΔδHα < 0.1 indicates a rondam coil and Δδ Hα < -0.1 ppm indicates a helical configuration. D. S. Wishart, B. D. Sykes, F. M. Richards, Biochemistry 1992, 31, 1647-1651.
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