Abstract

Overview

The study investigates the impact of high-frequency electromagnetic fields on the vibrational response of methyl (CH3) and methylene (CH2) groups in amino acids found in proteins when dissolved in water. This response was analyzed using Fourier Transform Infrared (FTIR) Spectroscopy.

Findings

• Experiments involved hemoglobin, bovine serum albumin, and myoglobin in solutions, exposed to electromagnetic fields emitted by mobile phones (Nokia 105 and Samsung GT-E1270).
• The exposure lasted for 4 hours to a power density of 0.95 W/m2 at 1750 MHz frequency.
• Significant increases in CH3 stretching vibrations were observed in myoglobin, indicating a stronger response due to its simpler protein chain structure.
• Conversely, CH2 stretching vibrations decreased in intensity across all proteins, suggesting a structural realignment of protein α-helices in response to the electromagnetic field.

Conclusion

The study highlights potential structural alterations in proteins subjected to electromagnetic fields, which could imply significant bio-molecular changes and emphasize the health risks associated with prolonged exposure to such fields.