Insights into the terahertz response of L-glutamic acid and its receptor

l-Glutamic acid (l-Glu) is a basic unit of proteins and also serves as an important neurotransmitter in the central nervous system. Its structural properties are critical for biological functions and selective receptor recognition. Although this molecule has been extensively studied, the low frequency vibrational behavior that is closely related to conformational changes and the intermolecular interactions between l-Glu and its receptors are still unclear. In this study, we acquired the fingerprint spectrum of l-Glu by using air plasma terahertz (THz) time-domain spectroscopy in the 0.5-18 THz range. The low frequency vibrational characteristics of l-Glu were investigated through density functional theory (DFT) calculations. The THz responses of the ligand binding domain of the NMDAR-l-Glu complex were studied by the ONIOM method, with a focus on discussing the normal modes and interactions of ligand l-Glu and water molecules. The results illustrate that THz spectroscopy exhibits a sensitive response to the influence of l-Glu on the structure of the NMDAR. The water molecules in proteins have various strong vibration modes in the THz band, showing specificity, diversity and complexity of vibrational behavior. There is potential for influencing and regulating the structural stability of the NMDAR-l-Glu complex through water molecules.