Hydrogen bond perturbation in hen egg white lysozyme by external electromagnetic fields: a nonequilibrium molecular dynamics study.
Solomentsev GY, English NJ, Mooney DA · 2010
View Original AbstractMicrowave radiation disrupts protein structure by breaking hydrogen bonds, showing how EMF exposure could interfere with essential biological processes.
Plain English Summary
Researchers used computer simulations to study how microwave radiation (2.45 to 100 GHz) affects the structure of lysozyme, a protein found in egg whites. They found that the electromagnetic fields disrupted hydrogen bonds that help maintain the protein's shape, with the most damage occurring on the protein's outer surface where bonds are naturally weaker. This demonstrates that microwave radiation can alter protein structure at the molecular level, potentially affecting how proteins function in living systems.
Why This Matters
This molecular-level research provides crucial insight into how microwave radiation interacts with biological systems. The study demonstrates that electromagnetic fields in the 2.45 to 100 GHz range can disrupt hydrogen bonds in proteins, which are fundamental to maintaining proper protein structure and function. What makes this particularly relevant is that 2.45 GHz is the same frequency used by microwave ovens and WiFi devices. While this was a computer simulation using a single protein type, it reveals a plausible mechanism by which RF radiation could affect biological processes. The finding that weaker, surface-exposed hydrogen bonds are most vulnerable suggests that proteins in living cells could experience similar structural disruptions when exposed to microwave radiation, potentially affecting cellular function and health.
Exposure Information
Specific exposure levels were not quantified in this study. The study examined exposure from: 2.45 to 100 GHz
Study Details
Nonequilibrium molecular dynamics simulations of a charge-neutral mutant of hen egg white lysozyme have been performed at 300 K and 1 bar in the presence of external microwave fields (2.45 to 100 GHz) of an rms electric field intensity of 0.05 V Å(-1).
A systematic study was carried out of the distributions of persistence times and energies of each i...
It was found that localized translational motion for formally charged residues led to greater disrup...
Show BibTeX
@article{gy_2010_hydrogen_bond_perturbation_in_2583,
author = {Solomentsev GY and English NJ and Mooney DA},
title = {Hydrogen bond perturbation in hen egg white lysozyme by external electromagnetic fields: a nonequilibrium molecular dynamics study.},
year = {2010},
url = {https://pubmed.ncbi.nlm.nih.gov/21186890/},
}