{Reference Type}: Journal Article
{Title}: Far-infrared terahertz properties of L-cysteine and its hydrochloride monohydrate.
{Author}: Ren G;Zong S;Zhu Z;Cheng C;Chen L;Zhou L;Zhang J;Liu L;Han J;Zhao H;
{Journal}: Spectrochim Acta A Mol Biomol Spectrosc
{Volume}: 225
{Issue}: 0
{Year}: Jan 2020 15
{Factor}: 4.831
{DOI}: 10.1016/j.saa.2019.117476
{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.