research article
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
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.
Type
research article
Author(s)
Date Issued
2003
Publisher
Published in
Volume
42
Issue
13
Start page
1534
End page
1537
Editorial or Peer reviewed
REVIEWED
Written at
OTHER
EPFL units
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