Nonthermal acceleration of protein hydration by sub-terahertz irradiation

The collective intermolecular dynamics of protein and water molecules, which overlap in the sub-terahertz (THz) frequency region, are relevant for expressing protein functions but remain largely unknown. This study used dielectric relaxation (DR) measurements to investigate how externally applied sub-THz electromagnetic fields perturb the rapid collective dynamics and influence the considerably slower chemical processes in protein-water systems. We analyzed an aqueous lysozyme solution, whose hydration is not thermally equilibrated. By detecting time-lapse differences in microwave DR, we demonstrated that sub-THz irradiation gradually decreases the dielectric permittivity of the lysozyme solution by reducing the orientational polarization of water molecules. Comprehensive analysis combining THz and nuclear magnetic resonance spectroscopies suggested that the gradual decrease in the dielectric permittivity is not induced by heating but is due to a slow shift toward the hydrophobic hydration structure in lysozyme. Our findings can be used to investigate hydration-mediated protein functions based on sub-THz irradiation. The collective intermolecular dynamics of protein and water molecules, which overlap in subterahertz frequencies, are relevant for protein function expressions. Here the authors develop highly sensitive dielectric measurements, revealing that protein hydration is nonthermally accelerated by sub-terahertz irradiation.

Automated summary

This study investigates the collective dynamics of protein and water molecules in the sub-terahertz frequency region and their influence on the chemical processes in protein-water systems. The results show that sub-terahertz irradiation gradually decreases the dielectric permittivity of the protein solution by reducing the polarization of water molecules. These findings are important for studying hydration-mediated protein functions based on sub-terahertz irradiation.