F. Mancinelli, M. Caraglia, A. Abbruzzese, G. d’Ambrosio, R. Massa and E. Bismuto, “Non-Thermal Effects of Electromagnetic Fields at Mobile Phone Frequency on the Refolding of an Intracellular Protein: Myoglobin,” Journal of Cellular Biochemistry, Vol. 93, No. 1, 1 September 2004, pp. 188-196.

has been cited by the following article:

• TITLE: Inspections of Mobile Phone Microwaves Effects on Proteins Secondary Structure by Means of Fourier Transform Infrared Spectroscopy

  AUTHORS: Emanuele Calabrò, Salvatore Magazù

  KEYWORDS: Mobile Phone, Microwaves, Protein, Infrared Spectrum, Secondary Structure, Amide I

  JOURNAL NAME: Journal of Electromagnetic Analysis and Applications, Vol.2 No.11, December 1, 2010

  ABSTRACT: In this study the effects of microwaves on the secondary structure of three typical proteins have been investigated. A set of samples of lysozyme, bovine serum albumin and myoglobin in D2O solutions were exposed for 8 hours to mobile phone microwaves at 900 MHz at a magnetic field intensity around 16 mA/m. The relative effects on the secondary structure of the proteins were studied by means of Fourier Transform Infrared Spectroscopy. An increase of the amide I band intensity in the secondary structure of the proteins was observed after the microwaves exposure. Furthermore, a weak shift of the amide I mode of bovine serum albumin and a heavier shift of the amide I of myoglobin occurred after the exposure. In addition, a clear increasing of the β-sheet components with respect to the α-helix content was observed in the spectra of bovine serum albumin and myoglobin after the exposure, suggesting the hypothesis of the formation of aggregates.