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Unprecedented Torsional Preferences in trans2,3-Amino Acid Residues and Formation of 11-Helices in α,β2,3-Hybrid Peptides

Authors

  • Dhayalan Balamurugan,

    1. Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India), Fax: (+91) 44-2257-4202
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  • Dr. Kannoth M. Muraleedharan

    Corresponding author
    1. Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India), Fax: (+91) 44-2257-4202
    • Department of Chemistry, Indian Institute of Technology Madras, Chennai, 600036 (India), Fax: (+91) 44-2257-4202
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Abstract

original image

Anti or gauche? trans2,3-Amino acid residues that are known to promote extended structures in their peptides show specific rotamer preferences in response to an intramolecular hydrogen-bonding possibility, which facilitates the 11-helical structures in their 1:1 α,β-hybrid peptides (see figure). Preferences for the gauche conformation for all internal β residues and anti for the C-terminal residue in these peptides were confirmed by NMR spectroscopic and X-ray diffraction experiments.

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