Abstract
Infrared (IR) and terahertz (THz) spectroscopy simulations were carried out using CHARMM35b2 to determine protein stability. The stabilities of three hyperthermophilic 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.
| Original language | English |
|---|---|
| Article number | 7811291 |
| Pages (from-to) | 131-141 |
| Number of pages | 11 |
| Journal | IEEE Transactions on Terahertz Science and Technology |
| Volume | 7 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Mar 2017 |
| Externally published | Yes |
Keywords
- Cold shock proteins (Csps)
- desolvation spectra
- molecular dynamics
- thermologues
- vibrational modes
ASJC Scopus subject areas
- Radiation
- Electrical and Electronic Engineering