Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism

E. Schwartz, E. Schwartz, V. Liegeois, M. Koepf, P. Bodis, Jeroen Johannes Lambertus Maria Cornelissen, P. Brocorens, D. Beljonne, R.J.M. Nolte, A.E. Rowan, S. Woutersen, B. Champagne

Research output: Contribution to journalArticleAcademicpeer-review

14 Citations (Scopus)

Abstract

Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the C[DOUBLE BOND]N-stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amide I and amide II modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices.
Original languageEnglish
Pages (from-to)13168-13174
Number of pages6
JournalChemistry: a European journal
Volume19
Issue number39
DOIs
Publication statusPublished - 2013

Keywords

  • IR-90144
  • METIS-301670

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