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Inside Cover: Exploiting Aromatic Interactions for β‐Peptide Foldamer Helix Stabilization: A Significant Design Element (Chem. Eur. J. 16/2014)
Author(s) -
Mándity István M.,
Monsignori Antonella,
Fülöp Lívia,
Forró Enikö,
Fülöp Ferenc
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201490063
Subject(s) - foldamer , helix (gastropod) , peptide , chemistry , cover (algebra) , stereochemistry , crystallography , biochemistry , biology , engineering , mechanical engineering , ecology , snail
The self‐association of tetrameric helical oligomers in the form of vesicles has been observed for the first time while investigating helix stabilization through application of aromatic side‐chains in β‐peptide oligomers. For more details, see the Full Paper by F. Fülöp and et al. on page 4591 ff.