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Mimicry of a ?-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer.


ABSTRACT: The design and characterization of a proteomimetic foldamer that displays lateral flexibility endowed by intramolecular bifurcated hydrogen bonds is reported. The MAMBA scaffold, derived from meta-aminomethylbenzoic acid, adopts a serpentine conformation that mimics the side chain projection of all four residues in a ?-hairpin turn.

SUBMITTER: Meisel JW 

PROVIDER: S-EPMC6047514 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

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Mimicry of a β-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer.

Meisel Joseph W JW   Hu Chunhua T CT   Hamilton Andrew D AD  

Organic letters 20180613 13


The design and characterization of a proteomimetic foldamer that displays lateral flexibility endowed by intramolecular bifurcated hydrogen bonds is reported. The MAMBA scaffold, derived from meta-aminomethylbenzoic acid, adopts a serpentine conformation that mimics the side chain projection of all four residues in a β-hairpin turn. ...[more]

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