Investigation of the Correlations between Amino Acids, Amino Acid Mixtures and Dipeptides by Terahertz Spectroscopy

Terahertz Absorption Properties of Two Solid Amino Acids and Their Aqueous Solutions

“…Water is the source of life, and the formation of the protein liquid state is typically accompanied by the solvation effect of its various structures, in which the polypeptides in the chain of aqueous solution have higher flexibility, which makes the conformational transformation of proteins more agile, and the hydrophobicity of amino acids is conducive to the formation of the stable folding structure of protein [4]. It has been confirmed that THz spectroscopy can effectively be used to analyse the relationships between amino acids, amino acid mixtures, dipeptides and identified dipeptides, and their isomers at the molecular level [5]. Kutteruf et al [6] studied the terahertz spectra of solid-state short-chain peptide sequences and found that most of the spectral and structural information of the system was in the range of 1-15 THz.…”

Terahertz spectroscopy for interpreting the formation and hierarchical structures of silk fibroin oligopeptides

“…The system has been described in detail in previous works. 37 The samples were placed into the THz system and the relative humidity was less than 3% under nitrogen gas atmosphere.…”

Hydration Dynamics in Biological Membranes: Emerging Applications of Terahertz Spectroscopy

“…Incidentally, such a Hydration sheaths associated with biomimetic and biological membranes are expected to be particularly amenable to THzbased studies investigating spatial heterogeneity in the water hydrogen-bond network because of the rich tapestry of existing knowledge regarding membrane organization and dynamics. strategy has been successfully employed for THz-based studies of proteins, with systematic characterization of hydration of individual amino acids, 100 amino acid mixtures and dipeptides, 101 and peptide tetramers 102 complementing investigations on more complex biologically relevant proteins, 61,103−105 including GPCRs 106 and the SecY translocon. 107 In this context, we have recently explored the microstructure and collective dynamics of the water hydrogen-bond network associated with zwitterionic and negatively charged model membrane bilayers as a function of lipid concentration using THz-TDS.…”

“…However, gaining quantitative insights on membrane hydration dynamics in complex cellular systems is strongly contingent on the availability of comprehensive literature on changes in THz patterns with differences in microenvironment (including pH and presence of salt, metal ions, and small molecules) commonly experienced by biological membranes. Incidentally, such a strategy has been successfully employed for THz-based studies of proteins, with systematic characterization of hydration of individual amino acids, amino acid mixtures and dipeptides, and peptide tetramers complementing investigations on more complex biologically relevant proteins, ,− including GPCRs and the SecY translocon …”