Effects of external electromagnetic fields on the conformational sampling of a short alanine peptide.
Solomentsev GY, English NJ, Mooney DA · 2012
View Original AbstractComputer simulations show 2.45 GHz radiation disrupts protein structure by interfering with hydrogen bonds that maintain protein stability.
Plain English Summary
Researchers used computer simulations to study how 2.45 GHz microwave radiation (the same frequency used in WiFi and microwave ovens) affects protein structure at the molecular level. They found that electromagnetic fields disrupted the normal folding patterns of proteins by interfering with hydrogen bonds that keep proteins stable. This suggests that microwave radiation can alter fundamental biological processes by changing how proteins maintain their shape and function.
Why This Matters
This molecular-level research provides crucial insight into how electromagnetic fields interact with the basic building blocks of life. While this was a computer simulation rather than a biological study, it demonstrates a plausible mechanism by which 2.45 GHz radiation could affect cellular function. The electric field strengths used (0.01-0.05 V/Å) are extremely high compared to typical environmental exposures, but the finding that EMF can disrupt protein hydrogen bonding aligns with other research showing biological effects from radiofrequency radiation. What makes this study particularly significant is that it identifies a specific pathway through which EMF could interfere with normal cellular processes. Proteins must maintain precise shapes to function properly, and any disruption to their folding patterns could have cascading effects on cellular health.
Exposure Details
- Electric Field
- 100,000,000 - 500,000,000 V/m
- Source/Device
- 2.45 GHz
Exposure Context
This study used 100,000,000 - 500,000,000 V/m for electric fields:
- 333.3Mx above the Building Biology guideline of 0.3 V/m
Building Biology guidelines are practitioner-based limits from real-world assessments. BioInitiative Report recommendations are based on peer-reviewed science. Check Your Exposure to compare your own measurements.
Study Details
Non-equilibrium molecular dynamics simulations of a solvated 21-residue polyalanine (A21) peptide, featuring a high propensity for helix formation, have been performed at 300 K and 1 bar in the presence of external electromagnetic (e/m) fields in the microwave region (2.45 GHz) and an r.m.s. electric field intensity range of 0.01–0.05 V/Å.
To investigate how the field presence affects transitions between the conformational states of a pro...
We observe folding-behavior of the peptide consistent with prior simulation and experimental studies...
Show BibTeX
@article{gy_2012_effects_of_external_electromagnetic_1334,
author = {Solomentsev GY and English NJ and Mooney DA},
title = {Effects of external electromagnetic fields on the conformational sampling of a short alanine peptide.},
year = {2012},
doi = {10.1002/jcc.22912},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/jcc.22912},
}