Beta Sheets with a Twist: The Conformation of Helical Polyisocyanopeptides Determined by Using Vibrational Circular Dichroism. Issue 39 (12th August 2013)

• Record Type: Journal Article
• Authors: Schwartz, Erik; Liégeois, Vincent; Koepf, Matthieu; Bodis, Pavol; Cornelissen, Jeroen J. L. M.; Brocorens, Patrick; Beljonne, David; Nolte, Roeland J. M.; Rowan, Alan E.; Woutersen, Sander; Champagne, Benoît
• Is Part Of: Chemistry. Volume 19:Issue 39(2013)
• Page Start: 13168
• Page End: 13174
• Publication Date: 2013-08-12
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201300073
• Languages: English
• ISSNs: 0947-6539

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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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.</p> </abstract>