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Globule to helix transition in sodiated polyalanines

  • Jonathan K. Martens
  • , Isabelle Compagnon
  • , Edith Nicol
  • , Terry B. McMahon
  • , Carine Clavaguéra
  • , Gilles Ohanessian
  • CNRS
  • Department of Chemistry
  • University of Waterloo
  • University of Lyon
  • IGFL, Université de Lyon, Université Lyon 1
  • Centre national de la recherche scientifique

Research output: Contribution to journal › Article › peer-review

36 Citations (Scopus)

Abstract

The structures of sodiated polyalanine peptides containing 8-12 residues are investigated using infrared multiple photon dissociation (IRMPD) spectroscopy and classical and quantum modeling. Calculations indicate that the α-helical structure is the most stable conformation for the peptides whatever their size. The IRMPD spectra provide evidence for the coexistence of helical and globular shapes for Ala8Na+, and possibly for Ala9Na+. The turning point from globule to helix is thus found at Ala8-9Na+. The N-H and O-H stretching region allows identifying a new spectroscopic pattern typical for α-helical structures of polyalanines.

Original languageEnglish
Pages (from-to)3320-3324
Number of pages5
JournalJournal of Physical Chemistry Letters
Volume3
Issue number22
DOIs
Publication statusPublished - 15 Nov 2012
Externally publishedYes

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