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

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.