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- W2809974577 abstract "Single residue control of the helical topology of β-peptides is a contemporary challenge in foldamer science. We present the conformational preferences of oligomers of trans-2-aminocyclobutanecarboxylic acid (tACBC), in which a central residue has been replaced by a single N-aminoazetidine-2-carboxylic acid (AAzC) moiety. The latter has such a strong demand for local 8-helical conformers that the usual 12-helix secondary structure of a tACBC octamer is switched to a fully 8-helical conformation as a result of the single residue substitution." @default.
- W2809974577 created "2018-07-10" @default.
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- W2809974577 date "2018-07-02" @default.
- W2809974577 modified "2023-10-18" @default.
- W2809974577 title "Strategic C to N Replacement in β-Peptides: Atomic Level Control of Helical Folding" @default.
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- W2809974577 doi "https://doi.org/10.1021/acs.joc.8b01096" @default.
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