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- W2019628323 abstract "Conformational analysis of N-acetylated hexapeptide mimics incorporating a bicyclic lactam (1-4) was carried out by a combination of 1H-NMR spectroscopy, IR spectroscopy, and computer modeling. The nature of the bicyclic lactam determines the turn motifs and the folding patterns of these constrained peptides. The (5,6)-bicyclic lactam derivatives 1 and 2, characterized by a type-II' β-turn (CO3···H6-N), are very compact intramolecularly H-bonded structures. The (5,7)-bicyclic lactam derivative 3, characterized by an inverse γ-turn (CO4···H6-N), is a quite flexible “tweezer-like” structure." @default.
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- W2019628323 date "2000-03-01" @default.
- W2019628323 modified "2023-10-17" @default.
- W2019628323 title "Rationally Designed Bicyclic Lactams Control Different Turn Motifs and Folding Patterns in Hexapeptide Mimics" @default.
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- W2019628323 doi "https://doi.org/10.1002/(sici)1099-0690(200003)2000:5<695::aid-ejoc695>3.0.co;2-v" @default.
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