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

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.

KEYWORDS:

• Proteins
• amino acids
• FTIR spectroscopy
• methyl
• methylene
• stretching vibrations
• dipole moment

Declaration of Interest

The authors declare that there is no conflict of interest regarding the publication of this paper.