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- W3014372023 endingPage "6171" @default.
- W3014372023 startingPage "6165" @default.
- W3014372023 abstract "Rational control of the self-organization of β-peptides sequences to adopt regular secondary structures is an important challenge in peptidomimetic foldamer science. By replacing the N- and C-terminal residues of homooligomers of trans-2-aminocyclobutanecarboxylic acid (tACBC)n with N-aminoazetidine-2-carboxylic acid, an 8-helical topology is shown to dominate for sequences up to n = 7. This constitutes an atomic-level tool to override locally the preferred global 12-helix secondary structure of the corresponding tACBC homooligomers of the same length." @default.
- W3014372023 created "2020-04-10" @default.
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- W3014372023 date "2020-04-01" @default.
- W3014372023 modified "2023-10-14" @default.
- W3014372023 title "Local versus Global Control of Helical Folding in β-Peptide Segments Using Hydrazino Turns" @default.
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- W3014372023 doi "https://doi.org/10.1021/acs.joc.0c00305" @default.
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