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Two Helical Conformations from a Single Foldamer Backbone: “Split Personality” in Short α/β‐Peptides
Author(s) -
Hayen Ahlke,
Schmitt Margaret A.,
Ngassa Felix N.,
Thomasson Kathryn A.,
Gellman Samuel H.
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352125
Subject(s) - foldamer , monomer , oligopeptide , chemistry , amino acid , peptide , type (biology) , stereochemistry , crystallography , biochemistry , organic chemistry , biology , polymer , ecology
Oligopeptides with heterogeneous backbones , i.e., oligopeptides containing more than one monomer type, may be a fruitful source of new foldamers. This conclusion was suggested by studies on oligomers comprising L ‐α‐amino acid and cyclic β‐amino acid residues in a sequentially alternating pattern, which are shown to display helical secondary structure in solution.