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Polypeptide Helices in Hybrid Peptide Sequences

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https://figshare.com/articles/dataset/Polypeptide_Helices_in_Hybrid_Peptide_Sequences/3254302
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A new class of polypeptide helices in hybrid sequences containing α-, β-, and γ-residues is described. The molecular conformations in crystals determined for the synthetic peptides Boc-Leu-Phe-Val-Aib-βPhe-Leu-Phe-Val-OMe 1 (βPhe:  (S)-β3-homophenylalanine) and Boc-Aib-Gpn-Aib-Gpn-OMe 2 (Gpn:  1-(aminomethyl)cyclohexaneacetic acid) reveal expanded helical turns in the hybrid sequences (ααβ)n and (αγ)n. In 1, a repetitive helical structure composed of C14 hydrogen-bonded units is observed, whereas 2 provides an example of a repetitive C12 hydrogen-bonded structure. Using experimentally determined backbone torsion angles for the hydrogen-bonded units formed by hybrid sequences, we have generated energetically favorable hybrid helices. Conformational parameters are provided for C11, C12, C13, C14, and C15 helices in hybrid sequences.
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2016-05-05
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