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A novel peptide conformation: the γ-bend ribbon

Abstract : Unlike the extensively investigated relationship between the peptide β-bend ribbon and its prototypical 310-helix conformation, the corresponding relationship between the narrower γ-bend ribbon and its regular γ-helix counterpart still remains to be studied, as the latter 3D-structures have not yet been experimentally authenticated. In this paper, we describe the results of the first characterization, both in the crystal state and in solution, of the γ-bend ribbon conformation using X-ray diffraction and FT-IR absorption, electronic CD and 2D-NMR spectroscopies applied to an appropriate set of synthetic, homo-chiral, sequential dipeptide oligomers based on (S)-Ala and the known γ-bend inducer, Cα-tetrasubstituted, N-alkylated α-amino acid residue (S)-Cα-methyl-azetidine-carboxylic acid.
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https://hal.archives-ouvertes.fr/hal-02348893
Contributor : Karen Wright Connect in order to contact the contributor
Submitted on : Tuesday, November 5, 2019 - 2:44:37 PM
Last modification on : Wednesday, November 3, 2021 - 6:03:43 AM

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Bruno Drouillat, Cristina Peggion, Barbara Biondi, Karen Wright, François Couty, et al.. A novel peptide conformation: the γ-bend ribbon. Organic and Biomolecular Chemistry, Royal Society of Chemistry, 2018, 16 (42), pp.7947-7958. ⟨10.1039/c8ob02279h⟩. ⟨hal-02348893⟩

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