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

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ID: 27575
2019
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Ranked #87 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 Guanhua Ren, Siqi Zong, Zhongjie Zhu, Chao Cheng, Ligang Chen, Lu Zhou, Jianbing Zhang, Liyuan Liu, Jiaguang Han, Hongwei Zhao
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Journal spectrochimica acta part a, molecular and biomolecular spectroscopy
Year 2019
DOI
S1386-1425(19)30866-2
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