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Stable Helical Secondary Structure in Short‐Chain N , N ′‐Linked Oligoureas Bearing Proteinogenic Side Chains
Author(s) -
Semetey Vincent,
Rognan Didier,
Hemmerlin Christine,
Graff Roland,
Briand JeanPaul,
Marraud Michel,
Guichard Gilles
Publication year - 2002
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 - 10.1002/1521-3773(20020603)41:11<1893::aid-anie1893>3.0.co;2-f
Subject(s) - protein secondary structure , chemistry , side chain , peptide , service (business) , crystallography , hydrogen bond , stereochemistry , helix (gastropod) , bearing (navigation) , computer science , molecule , biochemistry , biology , business , organic chemistry , artificial intelligence , ecology , marketing , snail , polymer
Closely related to the ( P )2.6 14 helix of γ ‐peptides : Heptamer 1 bearing side chains of Ala, Val, and Tyr adopts a stable 2.5‐helical secondary structure in solution that is characterized by a pitch of approximately 5.1 Å and by the simultaneous presence of 12‐ and 14‐membered hydrogen‐bonded rings. Thus N , N ′‐linked oligoureas belong to the growing family of non‐natural non‐peptide oligomers with defined and predictable secondary structure.