Investigating Biomolecular Interactions using Terahertz Pulsed Spectroscopy

The bio-molecular interaction has been one of the most challenging subjects to probe due to its complexity. In the thesis, we have been attempting to answer fundamental questions about bio-molecular interactions in the terahertz (THz) region from the macroscopic to microscopic level. Terahertz radiation (defined as 0.1--10 THz) can excite intermolecular interactions such as the librational and vibrational modes. These attributes make it feasible to probe the dynamic characteristics of the bio-molecular system. Furthermore, it is worth investigating whether terahertz technology could potentially be used as a novel tool in the biomedical diagnosis field in the near future.;We develop a controlled study to investigate the effects of formalin fixing on the THz properties of two different tissue types. The optical properties are measured using THz reflection spectroscopy. The results present how the fixing process can affect image contrast in THz images of biological samples.;Secondly, we focus our aims on investigating protein molecules due to the possibility of being able to explain the mechanism of molecular interactions more clearly. Two lands of labeled immunoglobulin G were investigated using a reflective THz-IDS system. The dielectric properties were sensitive to the conjugation of the antibody. Additionally, terahertz spectroscopy is able to evaluate the depth of the hydrogen shell and shows that the hydrogen-bonded networks of charged protein solutions play an important role in determining the dielectric.;Thirdly, using a transmission THz-TDS system we investigated a biomarker protein and observed distinct spectral differences at various temperatures. This work demonstrates that terahertz spectroscopy can be used to evaluate the anharmonicity of the vibrational potential. By comparing the absorption spectra of the THz-TDS and Synchrotron results it is possible to deduce the approximate localization of the vibrational modes within the molecular chain.;Finally, based on theoretical calculations and experiments, we present a development model (DDRA model) to describe the interaction between the protein and its solvent molecule. The parameters derived from this model provide good fits to the experimentally determined complex dielectric constant, making it of the model valuable benchmarks for other theoretical treatments of bio-molecular system.