Investigations of the water clusters of the protected amino acid Ac-Phe-OMe by applying IR/UV double resonance spectroscopy: microsolvation of the backbone
| Autor: | Kirsten Schwing, Holger Fricke, A. Gerlach, Markus Gerhards, C. Unterberg |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
Spectrophotometry
Infrared Chemistry Ab initio Solvation Water General Physics and Astronomy Resonance (chemistry) Crystallography chemistry.chemical_compound Solvation shell Monomer Ab initio quantum chemistry methods Computational chemistry Amide Molecule Spectrophotometry Ultraviolet Amino Acids Physical and Theoretical Chemistry |
| Zdroj: | Physical Chemistry Chemical Physics. 12:3511 |
| ISSN: | 1463-9084 1463-9076 |
| DOI: | 10.1039/c000424c |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|