期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 12, 期 14, 页码 3511-3521出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c000424c
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资金
- Deutsche Forschungsgemeinschaft [DFG 961/3-3, GRK 792]
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.
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