Unfolding-induced in Haemoglobin by Exposure to Electromagnetic Fields: A FTIR Spectroscopy Study

" A decrease in intensity of the a-helix component in the amide I and amide II regions was observed after exposure of 4 h to a 50 Hz electromagnetic field at 1 mT. In addition, Fourier self deconvolution analysis was carried out on exposed and not-exposed spectra. A relative increase of the b-sheet feature in the amide I region was evidenced, showing that an unfolding process of the protein occurred after exposure to extremely low frequency electromagnetic field, suggesting the hypothesis of the formation of aggregates." {Credits 1}

Secondary structure of the protein is affected, and the paper references other studies where it is show that secondary structure of proteins is affected by extremely low frequencies and microwaves.

{Credits 1} 🎪 Calabro, E., & Magazu, S. (2014). Unfolding-Induced in Haemoglobin by Exposure to Electromagnetic Fields: a Ftir Spectroscopy Study. Oriental Journal of chemistry, 30(1), 31-35. © 2014 The Author(s). This article is licensed under a Creative Commons Attribution License.

Last modified on 03-May-17

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