descriptionPublicationkeyboard_double_arrow_right Article 03 Nov 2005 English Publisher:American Chemical Society (ACS)Journal:Journal of the American Chemical Society, volume 127, pages 16,668-16,674 (issn: 0002-7863, eissn: 1520-5126,

Authors: Ananda, Kuppanna; Vasudev, Prema G; Sengupta, Anindita; Poopathi Raja, K Muruga; Shamala, Narayanaswamy; Balaram, Padmanabhan;

doi: 10.1021/ja055799z

pmid: 16305256

Polypeptide Helices in Hybrid Peptide Sequences

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Abstract

A new class of polypeptide helices in hybrid sequences containing alpha-, beta-, and gamma-residues is described. The molecular conformations in crystals determined for the synthetic peptides Boc-Leu-Phe-Val-Aib-betaPhe-Leu-Phe-Val-OMe 1 (betaPhe: (S)-beta3-homophenylalanine) and Boc-Aib-Gpn-Aib-Gpn-OMe 2(Gpn: 1-(aminomethyl)cyclohexaneacetic acid) reveal expanded helical turns in the hybrid sequences (alpha alphabeta)n and (alphagamma)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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Molecular Structure, Protein Conformation, Helix-Loop-Helix Motifs, Computer Simulation, Hydrogen Bonding, Molecular Biophysics Unit, Peptides, Protein Structure, Secondary

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CCDC 271599: Experimental Crystal Structure Determination
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CCDC 271598: Experimental Crystal Structure Determination
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