TU Kaiserslautern, Fachbereich Chemie and research center OPTIMAS, Erwin-Schrödinger-Strasse 52, 67663 Kaiserslautern, Germany.
Phys Chem Chem Phys. 2010 Apr 14;12(14):3511-21. doi: 10.1039/c000424c. Epub 2010 Mar 10.
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.
为了研究水合作用对肽或保护氨基酸主链的影响，采用红外/紫外双共振光谱法分析了 Ac-Phe-OMe 的连续水合作用。为了得到有意义的结果，我们在酰胺 A 和 OH 伸缩振动区域以及酰胺 I/II 模式下记录了光谱。与从头算和 DFT 计算的比较导致了具有尺寸选择性的结构分配。在分子束中观察到单水合和二水合簇的两种异构体以及三水合簇的一种异构体，从而形成了主链的第一个溶剂化壳。在三水合簇的情况下，与单体的结构相比，主链的几何形状发生了显著变化，因为可以形成水分子的网络。
