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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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Lösung Eine StabileProtein AssemblyStructural BioinformaticsMolecular BiologyPeptide ScienceAnalytical UltracentrifugationChemical BiologyProtein FoldingProtein X-ray CrystallographyDas Harnstoff-heptamer 1Nmr FacilitiesMacromolecular AssembliesProtein ChemistryBruker Drx 600BiochemistryBiomolecular AnalysisDna ReplicationSolution Nmr Spectroscopy2.5-Helicale Sekundärstruktur EinBiomolecular ScienceStructural BiologyBiomolecular EngineeringBruker Arx 500Natural SciencesPeptide SynthesisProtein NmrMolecular BiophysicsMedicine
Eng verwandt mit der (P)2.614-Helix von γ-Peptiden: Das Harnstoff-Heptamer 1 nimmt in Lösung eine stabile, 2.5-helicale Sekundärstruktur ein, die durch eine Ganghöhe von etwa 5.1 Å sowie 12- und 14-gliedrige Wasserstoffbrückenringe charakterisiert ist. N,N′-verknüpfte Oligoharnstoffe gehören somit zu der wachsenden Familie von nichtnatürlichen, nichtpeptidischen Oligomeren mit definierter und vorhersagbarer Sekundärstruktur. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2001/2002/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.