Issue 1, 2005
From the journal:

Physical Chemistry Chemical Physics

Vibrational spectroscopy of a non-aromatic amino acid-based model peptide: identification of the γ-turn motif of the peptide backbone

Isabelle Compagnon,*a   Jos Oomens,a   Joost Bakker,a   Gerard Meijerb  and  Gert von Heldenb  

* Corresponding authors

a FOM-Institute for Plasma Physics Rijnhuizen, Edisonbaan 14, Nieuwegein, The Netherlands

b Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4-6, Berlin, Germany

Abstract

The first infrared hole burning spectrum of a gas-phase neutral peptide not containing an aromatic amino acid is presented. In the model peptide Z–Pro–NHMe, the amide I and II bands in the 1500–1800 cm−1 region appear to be a clear diagnostic for the secondary structure of the backbone, while the analysis of a series of coupled CH bending modes in the 1000–1500 cm−1 region allows to distinguish between different possible orientations of the chromophore. The geometry of the peptide is strongly constrained by the proline and only one conformation of the backbone is observed, which is identified as a hydrogen bonded γ-turn.

Graphical abstract: Vibrational spectroscopy of a non-aromatic amino acid-based model peptide: identification of the γ-turn motif of the peptide backbone

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Article information

DOI
https://doi.org/10.1039/B417204C
Article type
Communication
Submitted
10 Nov 2004
Accepted
19 Nov 2004
First published
26 Nov 2004

Phys. Chem. Chem. Phys., 2005,7, 13-15

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Vibrational spectroscopy of a non-aromatic amino acid-based model peptide: identification of the γ-turn motif of the peptide backbone

I. Compagnon, J. Oomens, J. Bakker, G. Meijer and G. von Helden, Phys. Chem. Chem. Phys., 2005, 7, 13 DOI: 10.1039/B417204C

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