The α-helix alignment of proteins in water solution toward a high-frequency electromagnetic field: A FTIR spectroscopy study.
Calabrò E, Magazù S. · 2017
View Original AbstractMobile phone radiation physically realigns protein structures at cellular level, potentially disrupting fundamental biological processes.
Plain English Summary
Italian researchers exposed proteins (including hemoglobin and albumin) to mobile phone radiation at 1750 MHz for 4 hours and measured changes in their molecular structure. They found that the proteins' alpha-helix structures physically aligned themselves with the electromagnetic field, causing measurable changes in their chemical bonds. This demonstrates that cell phone-level radiation can directly alter the shape and orientation of essential biological molecules.
Why This Matters
This study provides direct molecular evidence that mobile phone radiation can physically restructure proteins at the cellular level. The researchers used a power density of 1 W/m² (1000 mW/m²), which is well within the range of typical mobile phone exposures during calls. What makes this research particularly significant is that it demonstrates a clear mechanism by which EMF exposure affects biological systems - the electromagnetic field literally forces protein molecules to realign themselves. Since proteins are fundamental to virtually every biological process in your body, from oxygen transport (hemoglobin) to immune function (albumin), this structural disruption could have far-reaching health implications. The science demonstrates that EMF effects on living systems aren't just theoretical - they're happening at the most basic molecular level.
Exposure Details
- Power Density
- 0.1 µW/m²
- Source/Device
- 1750 MHz
- Exposure Duration
- 4 hours
Exposure Context
This study used 0.1 µW/m² for radio frequency:
- 10Mx above the Building Biology guideline of 0.1 μW/m²
- 166.7Kx above the BioInitiative Report recommendation of 0.0006 μW/cm²
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.
Where This Falls on the Concern Scale
Study Details
The aim of this article was to study the effects of mobile phone electromagnetic waves at 1750 MHz on the Amide I and Amide II vibration bands of some proteins in bidistilled water solution by means of Fourier transform infrared (FTIR) spectroscopy and Fourier self-deconvolution (FSD) analysis. The proteins that were used for the experiment were hemoglobin, myoglobin, bovine serum albumin and lysozyme.
The exposure system consisted of microwaves emitted by an operational mobile phone at the frequency ...
The main result was that Amide I band of the proteins that were used increased significantly (p < 0....
This result can be explained assuming that the α-helix structure of the proteins aligned itself with the direction of the electromagnetic field due to the alignment of C = O stretching and N − H bending ligands that are oriented along with the α-helix axis that give rise to the Amide I mode.
Show BibTeX
@article{e_2017_the_helix_alignment_of_883,
author = {Calabrò E and Magazù S.},
title = {The α-helix alignment of proteins in water solution toward a high-frequency electromagnetic field: A FTIR spectroscopy study.},
year = {2017},
doi = {10.1080/15368378.2017.1328691},
url = {https://www.tandfonline.com/doi/abs/10.1080/15368378.2017.1328691},
}