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Stable Helical Secondary Structure in Short-Chain N,N′-Linked Oligoureas Bearing Proteinogenic Side Chains Access to both the Bruker ARX 500 facilities of the Service Commun de RMN (Faculté de Chimie, Strasbourg) and the Bruker DRX 600 NMR facilities of the Service Commun de Biophysicochimie des Interactions Moléculaires (Université Henri Poincaré, Nancy I) were deeply appreciated.
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2002
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Protein AssemblyStructural BioinformaticsMolecular BiologyPeptide ScienceAnalytical UltracentrifugationPredictable Secondary StructureProtein FoldingProtein X-ray CrystallographyNon-natural Non-peptide OligomersNmr FacilitiesMacromolecular AssembliesProtein ChemistryBruker Drx 600BiochemistryBiomolecular AnalysisDna ReplicationSolution Nmr SpectroscopyBiomolecular ScienceStructural BiologyBiomolecular EngineeringBruker Arx 500Natural SciencesProtein NmrMolecular BiophysicsSide ChainsMedicine
Closely related to the (P)2.614 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. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2002/z17991_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.