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Promotion of Folding in Hybrid Peptides through Unconstrained γ Residues: Structural Characterization of Helices in (αγγ)n and (αγα)n Sequences

Authors

  • Krishnayan Basuroy,

    1. Department of Physics, Indian Institute of Science, Bangalore-560 012 (India)
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  • Bhimareddy Dinesh,

    1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012 (India)
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  • Prof. Narayanaswamy Shamala,

    Corresponding author
    1. Department of Physics, Indian Institute of Science, Bangalore-560 012 (India)
    • Narayanaswamy Shamala, Department of Physics, Indian Institute of Science, Bangalore-560 012 (India)

      Padmanabhan Balaram, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012 (India)

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  • Prof. Padmanabhan Balaram

    Corresponding author
    1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012 (India)
    • Narayanaswamy Shamala, Department of Physics, Indian Institute of Science, Bangalore-560 012 (India)

      Padmanabhan Balaram, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012 (India)

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  • This work is supported by institutional grant-in-aid from the Department of Biotechnology (DBT), India. B.D. is supported by the award of a UGC-DSK Postdoctoral Fellowship from the University Grants Commission (UGC), India.

Abstract

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Der γ-Aminosäurerest γ4(R)Val führt selbst in kurzen (αγα)n-Sequenzen zu helicalen Strukturen. Eine gemischte C12/C14-Helix (in der Wasserstoffbrücken Ringe mit 12 bzw. 14 Atomen schließen) wird von der 12 Reste umfassenden (αγγ)4-Sequenz aufgebaut (rechts im Bild). Die (αγα)2-Sequenz mit 6 Resten (links), deren Rückgrat konformativ nicht eingeschränkt ist, faltet in eine C12/C10-Helix.

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