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A Nonpeptidic Reverse Turn that Promotes Parallel Sheet Structure Stabilized by CH⋅⋅⋅O Hydrogen Bonds in a Cyclopropane γ‐Peptide
Author(s) -
Jones Christopher R.,
Qureshi M. Khurram N.,
Truscott Fiona R.,
Hsu ShangTe Danny,
Morrison Angus J.,
Smith Martin D.
Publication year - 2008
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.200802648
Subject(s) - antiparallel (mathematics) , beta sheet , chemistry , dipeptide , hydrogen bond , protein secondary structure , turn (biochemistry) , cyclopropane , stereochemistry , amide , amino acid , folding (dsp implementation) , peptide , cyclic peptide , context (archaeology) , crystallography , molecule , ring (chemistry) , organic chemistry , biochemistry , paleontology , physics , quantum mechanics , magnetic field , electrical engineering , biology , engineering
A twist of fate : Parallel‐turn linkers comprising an amino acid derived alcohol conjoined with an aromatic amide through a flexible linkage adopt reverse‐turn conformations. Cyclopropane tetra‐ and hexapeptide analogues form a CH⋅⋅⋅O hydrogen‐bond‐stabilized parallel‐sheet conformation (see scheme). NMR studies confirm the presence of hydrogen bonds in these structures.