Terahertz Spectroscopy to Determine Cold Shock Protein Stability Upon Solvation and Evaporation—A Molecular Dynamics Study

Abstract

Infrared (IR) and Terahertz (THz) spectroscopy simulations were carried out using CHARMM35b2 to determine protein stability. The stabilities of three bacterial cold shock proteins (Csps) originating from mesophiles, thermophiles and hyper- thermophiles respectively were investigated in this study. The three different Csps were investigated by Normal-Mode analysis and Molecular Dynamics simulation of THz spectra using the Hessian matrix for solvated systems, interpreted in the harmonic approximation at optimum near-melting temperatures of each homologue, by incorporating differences in the hydrous and anhydrous states of the Csps. The results show slight variations in the large scale protein motion. However, the IR spectra of Csps observed at the low frequency saddle surface region, clearly distinguishes the thermophilic and mesophilic proteins based on their stability. Further studies on protein stability employing low-frequency collective modes have the potential to reveal functionally important conformational changes that are biologically significant.

Survey of terahertz photonics and biophotonics

“…THz imaging decreases both requirements, allowing researchers to see interactions at even smaller molecule sizes with rapid sampling durations. [129][130][131][132][133][134][135][136][137] One such example is depicted in Fig. 6, where THz imaging achieved the same accuracy as fluorine labeling for detecting the presence of streptavidin protein bonding.…”