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- W1968370831 abstract "With the aim of obtaining information on the effect induced by main-chain length and amino acid sequence on the type of helical structure adopted by naturally-occurring peptides rich in Cα,α-dialkylated residues, an infrared absorption and 1H nuclear magnetic resonance analysis of chloroform solutions of the protected 2–9 segment of the peptaibol antibiotics emerimicins III and IV,-(Aib)3-l-Val-Gly-l-Leu-(Aib)2-, and all related short sequences starting from both the N- and C-termini was performed. The results are consistent with the presence of folded structures of the β-bend type (in the shorter peptides) or 310-helices (in the longer peptides). Extent of formation and stability of the inter- and intramolecular H-bonds have been assessed as a function of concentration, temperature, addition of dimethylsulphoxide (DMSO) and the free radical 2,2,6,6-tetramethy-1-piperidinyloxy (TEMPO). At high peptide concentration both folded and helical structures tend to self-associate extensively. In the self-association process the N(1)H and N(2)H groups are those acting as H-bonding donors. These results agree well with those obtained in the solid state by X-ray diffraction on the octapeptide itself and selected short sequences." @default.
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- W1968370831 date "1985-12-01" @default.
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- W1968370831 title "Linear oligopeptides: peptaibol antibiotics — preferred conformation of the 2–9 segment of emerimicins III and IV and all related short sequences" @default.
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- W1968370831 doi "https://doi.org/10.1016/0141-8130(85)90050-9" @default.
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