Chain-length-dependent helical motifs and self-association of β-peptides with constrained side chains

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89 Citations (Scopus)

Abstract

Homo-oligomers constructed by using trans-2-aminocyclohexanecarboxylic acid monomers without protecting groups were studied. Both ab initio theory and NMR measurements showed that the tetramer tends to adopt a 10-helix motif, while the pentamer and hexamer form the known 14-helix. It was concluded that the conformationally constrained backbone is flexible enough to afford both 10-helical and 14-helical motifs, this observation in turn providing evidence of the true folding process. Self-association of the helical units was also detected, and the results of variable-temperature diffusion NMR measurements strongly suggested the presence of helical bundles in methanol solution.

Original languageEnglish
Pages (from-to)547-553
Number of pages7
JournalJournal of the American Chemical Society
Volume127
Issue number2
DOIs
Publication statusPublished - Jan 19 2005

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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