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Issue 1, 2009
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Spectroscopy and conformational preferences of gas-phase helices

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Abstract

We describe here a study of the spectroscopy of two peptides that we expect to be helical, Ac-Phe-(Ala)5-Lys-H+ and Ac-Phe-(Ala)10-Lys-H+, and one that we expect to be globular, Ac-Lys(H+)-Phe-(Ala)10, with the goal of identifying the spectral features characteristic of their secondary structure. Conformation-specific IR-UV double resonance spectroscopy in a cold ion trap, together with nitrogen-15 isotopic substitution, allow us to identify four conformers of the smaller helix. Infrared spectra in the OH and amide NH stretch regions, together with theoretical calculations, provide diagnostics of the presence of helical structure as well as details of the specific hydrogen bonding patterns within the helix. The assigned vibrational spectra presented here provide a benchmark for the ability of theory to predict the spectrum of a helical peptide.

Graphical abstract: Spectroscopy and conformational preferences of gas-phase helices

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Publication details

The article was received on 14 Aug 2008, accepted on 02 Oct 2008 and first published on 06 Nov 2008


Article type: Paper
DOI: 10.1039/B814143F
Citation: Phys. Chem. Chem. Phys., 2009,11, 125-132
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    Spectroscopy and conformational preferences of gas-phase helices

    J. A. Stearns, C. Seaiby, O. V. Boyarkin and T. R. Rizzo, Phys. Chem. Chem. Phys., 2009, 11, 125
    DOI: 10.1039/B814143F

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