Three samples of different hemoglobin aqueous solutions (from ten healthy donors) were exposed to a 50 Hz electromagnetic field (also with 50 mg/ml sucrose or trehalose) and measurements were performed after 3 h of exposure.
Proteins exist in different structures (e.g. beta-sheet and alpha-helix structure are typical secondary protein structures) generating different vibration bands within the FTIR spectroscopy (an infrared spectroscopy). Different amide bands originating from vibrations of the peptide or protein backbone are characteristic for protein vibration spectra.
Exposure duration: continuous for 3 h
|Exposure duration||continuous for 3 h|
|magnetic flux density||1 mT||-||measured||-||-|
The extremely low frequency electromagnetic field exposure affected infrared vibration bands of hemoglobin. Some changes, such as the relative increase in beta-sheet with respect to alpha-helix content in the amide I region, appeared barely perceptible, whereas an evident decrease in the intensity of the amide A band was observed after 3 h of exposure for haemoglobin in both water and aqueous sucrose solutions. In contrast, extremely low frequency electromagnetic fields did not affect the infrared spectrum of hemoglobin in trehalose solution, supporting the hypothesis of possible protective effects of disaccharides such as trehalose against extremely low frequency electromagnetic fields.