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Issue 14, 2010
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Investigations of the waterclusters of the protected amino acid Ac-Phe-OMe by applying IR/UV double resonance spectroscopy: microsolvation of the backbone

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Abstract

In order to investigate the influence of hydration on the backbone of a peptide or protected amino acid, the successive aggregation of water to Ac-Phe-OMe is analysed by means of IR/UV double resonance spectroscopy. To achieve meaningful results the spectra have been recorded in the region of the amide A and OH stretching vibrations as well as the amide I/II modes. Comparison with ab initio and DFT calculations leads to size-selective structural assignments. Two isomers of the mono- and dihydrated clusters and one isomer of the trihydrated cluster are observed in the molecular beam leading to a formation of the first solvation shell of the backbone. In case of the trihydrated cluster the backbone geometry is remarkably changed compared to the structure of the monomer since a network of water molecules can be formed.

Graphical abstract: Investigations of the water clusters of the protected amino acid Ac-Phe-OMe by applying IR/UV double resonance spectroscopy: microsolvation of the backbone

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Publication details

The article was received on 07 Jan 2010, accepted on 03 Mar 2010 and first published on 10 Mar 2010


Article type: Paper
DOI: 10.1039/C000424C
Phys. Chem. Chem. Phys., 2010,12, 3511-3521

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    Investigations of the water clusters of the protected amino acid Ac-Phe-OMe by applying IR/UV double resonance spectroscopy: microsolvation of the backbone

    H. Fricke, K. Schwing, A. Gerlach, C. Unterberg and M. Gerhards, Phys. Chem. Chem. Phys., 2010, 12, 3511
    DOI: 10.1039/C000424C

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