The fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues
Gademann, Karl; Hane, Andreas; Rueping, Magnus; Jaun, Bernhard; Seebach, Dieter
2003
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Abstract

The authors report compelling evidence for the formation of a fourth type of helical secondary structure of a beta-peptide in MeOH, and this phenomenon occurs if each amino acid has a hydroxy group in the 2-position. 2D-NMR expts. of terminally-protected beta-hexapeptide I were conducted to obtain its secondary structure information.

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Title The fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues
Author(s) Gademann, Karl ; Hane, Andreas ; Rueping, Magnus ; Jaun, Bernhard ; Seebach, Dieter
Published in Angewandte Chemie, International Edition
Volume 42
Issue 13
Pages 1534-1537
Date 2003
Keywords
DOI https://doi.org/10.1002/anie.200250290
Laboratories LSYNC
Record Appears in Scientific production and competences > SB - School of Basic Sciences > SB Archives > LSYNC - Chemical Synthesis Laboratory
Peer-reviewed publications
Work outside EPFL
Journal Articles
Published
Record creation date 2006-11-22

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