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Non-thermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: myoglobin.

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Mancinelli F, Caraglia M, Abbruzzese A, d'Ambrosio G, Massa R, Bismuto E · 2004

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Mobile phone radiation disrupted protein folding at exposure levels comparable to cell phone use, potentially affecting cellular function.

Plain English Summary

Summary written for general audiences

Italian researchers exposed myoglobin protein (found in muscle cells) to mobile phone frequency radiation for 3 hours and found it disrupted how the protein folded back into its proper shape. The electromagnetic fields slowed down the protein's natural folding process and altered its structural flexibility. This matters because proteins must fold correctly to function properly, and misfolded proteins are linked to various diseases.

Why This Matters

This study provides crucial evidence that mobile phone radiation can interfere with fundamental cellular processes at the molecular level. The researchers used myoglobin as a model protein because its structure is well-understood, making it an ideal test case for studying how electromagnetic fields affect protein behavior. What makes this particularly significant is that protein folding is essential for cellular function. When proteins don't fold correctly, they can clump together and become toxic to cells, a process implicated in neurodegenerative diseases like Alzheimer's and Parkinson's. The exposure level used (51 mW/g SAR) is within the range of what your body absorbs during mobile phone use, though the 3-hour continuous exposure represents an extreme scenario. The reality is that this research adds to a growing body of evidence showing that EMF exposure can disrupt biological processes even without heating tissue, challenging the outdated thermal-only safety standards still used by regulators today.

Exposure Details

SAR
51 W/kg
Source/Device
1.95 MHz
Exposure Duration
3 h

Exposure Context

This study used 51 W/kg for SAR (device absorption):

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 Exposure Level in ContextA logarithmic scale showing exposure levels relative to Building Biology concern thresholds and regulatory limits.Study Exposure Level in ContextThis study: 51 W/kgExtreme Concern0.1 W/kgFCC Limit1.6 W/kgEffects observed in the Extreme Concern range (Building Biology)FCC limit is 0x higher than this exposure level

Study Details

To study possible nonthermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: Myoglobin

Non-thermal effects induced by exposure to microwave electromagnetic field (MW-EMF) at 1.95 MHz, a f...

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These data suggest that MW-EMF could have also biochemical and, consequently, biological effects on eukaryotic cells that are still under investigation.

Cite This Study
Mancinelli F, Caraglia M, Abbruzzese A, d'Ambrosio G, Massa R, Bismuto E (2004). Non-thermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: myoglobin. J Cell Biochem. 93(1):188-196, 2004.
Show BibTeX
@article{f_2004_nonthermal_effects_of_electromagnetic_1177,
  author = {Mancinelli F and Caraglia M and Abbruzzese A and d'Ambrosio G and Massa R and Bismuto E},
  title = {Non-thermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: myoglobin.},
  year = {2004},
  
  url = {https://pubmed.ncbi.nlm.nih.gov/15352175/},
}

Quick Questions About This Study

Italian researchers exposed myoglobin protein (found in muscle cells) to mobile phone frequency radiation for 3 hours and found it disrupted how the protein folded back into its proper shape. The electromagnetic fields slowed down the protein's natural folding process and altered its structural flexibility. This matters because proteins must fold correctly to function properly, and misfolded proteins are linked to various diseases.