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Issue 48, 2009
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Gas phase folding of an (Ala)4 neutral peptide chain: spectroscopic evidence for the formation of a β-hairpin H-bonding pattern

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Abstract

IR and UV laser spectroscopy of an Ala-based 4-residue model peptide recorded under gas phase isolated conditions provides evidence for the intrinsic stability of compact folded structures resembling the extremity of a β-hairpin, with a C14H-bond bridging the two ends of the chain, and enables us to assess the capabilities of new quantum chemistry techniques to account for dispersive interactions in a medium-size molecule.

Graphical abstract: Gas phase folding of an (Ala)4 neutral peptide chain: spectroscopic evidence for the formation of a β-hairpin H-bonding pattern

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Publication details

The article was received on 09 Sep 2009, accepted on 14 Oct 2009 and first published on 02 Nov 2009


Article type: Communication
DOI: 10.1039/B918670K
Citation: Phys. Chem. Chem. Phys., 2009,11, 11385-11388
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    Gas phase folding of an (Ala)4 neutral peptide chain: spectroscopic evidence for the formation of a β-hairpin H-bonding pattern

    E. Gloaguen, R. Pollet, F. Piuzzi, B. Tardivel and M. Mons, Phys. Chem. Chem. Phys., 2009, 11, 11385
    DOI: 10.1039/B918670K

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