A study of a Cα, β-didehydroalanine homo-oligopeptide series in the solid-state by 13C cross-polarization magic angle spinning NMR

Authors

  • Katherine A. Henzler Wildman,

    1. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA
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  • Ayyalusamy Ramamoorthy,

    Corresponding author
    1. Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA
    2. Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109-1055, USA
    3. Macromolecular Science and Engineering, University of Michigan, Ann Arbor, MI 48109-1055, USA
    • Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA
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  • Tateaki Wakamiya,

    1. Department of Chemistry, Faculty of Science and Technology, Kinki University, Osaka 577, 8502 Japan
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  • Taichi Yoshikawa,

    1. Department of Chemistry, Faculty of Science and Technology, Kinki University, Osaka 577, 8502 Japan
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  • Marco Crisma,

    1. Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy
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  • Claudio Toniolo,

    1. Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy
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  • Fernando Formaggio

    1. Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy
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Abstract

The fully extended peptide conformation (2.05-helix) has been investigated for the first time in the solid-state by 13C cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on Cα, β-didehydroalanine. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.

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