Polypeptide helices in hybrid peptide sequences

Ananda, Kuppanna ; Vasudev, Prema G. ; Sengupta, Anindita ; Raja, K. Muruga Poopathi ; Shamala, Narayanaswamy ; Balaram, Padmanabhan (2005) Polypeptide helices in hybrid peptide sequences Journal of the American Chemical Society, 127 (47). pp. 16668-16674. ISSN 0002-7863

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Official URL: http://pubs.acs.org/doi/abs/10.1021/ja055799z

Related URL: http://dx.doi.org/10.1021/ja055799z


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.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:4327
Deposited On:13 Oct 2010 10:42
Last Modified:11 May 2012 11:21

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