Methyl and methylene vibrations response in amino acids of typical proteins in water solution under high- frequency electromagnetic field

2019 · Mixed · Low evidence

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MixedLow evidencePaper 1759

After 4 h exposure to a 1750 MHz field at 0.95 W/m2 emitted by operational mobile phones, CH3 stretching bands increased significantly in myoglobin in D2O solution. CH2 stretching vibrations decreased significantly in intensity for all exposed proteins.

Study snapshot

Publicationmanual · 2019

Study typein_vitro

Reported directionMixed

Evidence ratingLow

Abstract

Methyl and methylene vibrations response in amino acids of typical proteins in water solution under high- frequency electromagnetic field Calabrò E, Magazù S. Methyl and methylene vibrations response in amino acids of typical proteins in water solution under high-frequency electromagnetic field. Electromagn Biol Med. 2019 Jul 11:1-8. doi: 10.1080/15368378.2019.1641720. Abstract The aim of this paper was to study the response of methyl (CH3) and methylene (CH2) vibration bands in amino acids of some typical proteins diluted in bidistilled water solution after exposure to a high-frequency electromagnetic fields using Fourier Transform Infrared (FTIR) Spectroscopy. Hemoglobin in H2O solution and bovine serum albumin and myoglobin diluted in different D2O solutions were exposed for 4 h to a power density of 0.95 W/m2 at the frequency of 1750 MHz, emitted by operational mobile phones Nokia model 105 and Samsung model GT-E1270, in order to study the response of stretching vibrations of CH3 and CH2 that are in amino acids of those proteins. The main result was that CH3 stretching bands increased significantly in myoglobin in D2O solution because this protein is represented by a single protein chain so that the torque induced by the applied field is larger than that induced on the other two proteins. Otherwise, CH2 stretching vibrations decreased in intensity significantly for all exposed proteins. This result can be explained as well, assuming that, given a fixed volume, a decrease of population of CH2 occurred after exposure because of the alignment of proteins α-helices along the direction of the applied electromagnetic field. ncbi.nlm.nih.gov

Machine Enhanced Logic

AI evidence extraction

Structured fields below were generated from the paper’s abstract and metadata to make the evidence easier to inspect. Automated extraction may be incomplete or incorrect; verify important details against the original paper.

Study typein_vitro

Effect directionmixed

PopulationHemoglobin (H2O solution); bovine serum albumin and myoglobin (D2O solutions)

Sample sizeNot supplied

ExposureRF · 1750 MHz · 4 h

Evidence strengthLowConfidence: 78% · Peer reviewed: yes

Main findings

Outcomes measured

FTIR spectroscopy: CH3 (methyl) stretching vibration band intensity
FTIR spectroscopy: CH2 (methylene) stretching vibration band intensity

Limitations

Sample size and replication not reported in the abstract
Only biochemical/biophysical spectral outcomes reported; no health endpoints
Exposure metric limited to power density; SAR not reported
In vitro protein solutions (H2O/D2O), limiting generalizability to in vivo conditions

View raw extracted JSON

{
  "study_type": "in_vitro",
  "exposure": {
    "band": "RF",
    "source": "mobile phone",
    "frequency_mhz": 1750,
    "sar_wkg": null,
    "duration": "4 h"
  },
  "population": "Hemoglobin (H2O solution); bovine serum albumin and myoglobin (D2O solutions)",
  "sample_size": null,
  "outcomes": [
    "FTIR spectroscopy: CH3 (methyl) stretching vibration band intensity",
    "FTIR spectroscopy: CH2 (methylene) stretching vibration band intensity"
  ],
  "main_findings": "After 4 h exposure to a 1750 MHz field at 0.95 W/m2 emitted by operational mobile phones, CH3 stretching bands increased significantly in myoglobin in D2O solution. CH2 stretching vibrations decreased significantly in intensity for all exposed proteins.",
  "effect_direction": "mixed",
  "limitations": [
    "Sample size and replication not reported in the abstract",
    "Only biochemical/biophysical spectral outcomes reported; no health endpoints",
    "Exposure metric limited to power density; SAR not reported",
    "In vitro protein solutions (H2O/D2O), limiting generalizability to in vivo conditions"
  ],
  "evidence_strength": "low",
  "confidence": 0.78,
  "peer_reviewed_likely": "yes",
  "keywords": [
    "FTIR",
    "protein",
    "amino acids",
    "methyl vibrations",
    "methylene vibrations",
    "hemoglobin",
    "bovine serum albumin",
    "myoglobin",
    "D2O",
    "H2O",
    "RF-EMF",
    "mobile phone",
    "1750 MHz",
    "power density"
  ],
  "suggested_hubs": [
    {
      "slug": "mobile-phones-rf",
      "weight": 0.9,
      "reason": "Exposure described as 1750 MHz emitted by operational mobile phones."
    }
  ]
}

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AI-extracted fields are generated from the abstract and metadata and may be incomplete or incorrect. This material is for informational purposes and is not medical advice.

Identifiers and source

DOI: 10.1080/15368378.2019.1641720
PubMed: Not supplied

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