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Conformational structure and intermolecular interaction of phenylalanine by Raman spectroscopy in the CH stretching
Botao Yao1, Jialin Bai1, Xingyue Li1
1School of Physics, Xidian University, Xi'an 710071, China.
Abstract:
The structure of amino acids is of significance for the comprehension of protein functions. It is evident that traditional techniques have the capacity to yield precise structural information; however, it should be noted that these techniques are not without their limitations. Raman spectroscopy is highly sensitive to molecular structure; however, it is unable to provide accurate structural information in complex systems. In this study, the Raman spectra of phenylalanine in the CH stretching region were investigated. A comparison of the experimental Raman spectra of anhydrous phenylalanine, anhydrous phenylalanine (2-D), phenylalanine-H2O (3,3-D2), and the corresponding theoretical Raman spectra, revealed re-assigned vibrational bands in the CH stretching region, thereby resolving the controversy surrounding the spectral assignments. Furthermore, it was found that the CH stretching vibration of the methanetriyl group (>CH-) could be applied to identify the conformational structure and molecular interactions. This study proposes a potential spectroscopic probe for the detection of the structure and molecular interactions of phenylalanine in complex systems. And the deuterated methanetriyl group has the potential to facilitate in situ detection of dynamic structures and functions of proteins.
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