Far-infrared terahertz properties of L-cysteine and its hydrochloride monohydrate.

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ID: 27575
2019
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Ranked #85 of 116 articles by views in spectrochimica acta part a, molecular and biomolecular spectroscopy

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Abstract
As the building blocks of proteins, amino acids serve vital metabolic functions in addition to protein synthesis and thus attract enormous interest. Here we reported the far-infrared optical properties of L-cysteine (Lcys) and its hydrochloride monohydrate (LCHM) characterized by terahertz time-domain spectroscopy. The Lcys and LCHM exhibit quite distinct characteristics in the terahertz region due to diverse collective vibrations of the molecules, which is further confirmed by the solid-state density functional theory (DFT) calculations. The presented studies indicate that the intermolecular hydrogen bonds play a critical role in the far-infrared terahertz response of Lcys and LCHM.
Reference Key
ren2019farinfraredspectrochimica Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ren, Guanhua;Zong, Siqi;Zhu, Zhongjie;Cheng, Chao;Chen, Ligang;Zhou, Lu;Zhang, Jianbing;Liu, Liyuan;Han, Jiaguang;Zhao, Hongwei;
Journal spectrochimica acta part a, molecular and biomolecular spectroscopy
Year 2019
DOI
S1386-1425(19)30866-2
URL
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