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在暴露于1765兆赫微波的情况下,平行β-折叠振动带随蛋白质偶极矩增加。

Parallel β-sheet vibration band increases with proteins dipole moment under exposure to 1765 MHz microwaves.

作者信息

Calabrò Emanuele, Magazù Salvatore

机构信息

Department of Physics and Earth Sciences, University of Messina, Messina, Italy.

出版信息

Bioelectromagnetics. 2016 Feb;37(2):99-107. doi: 10.1002/bem.21956. Epub 2016 Feb 2.

DOI:10.1002/bem.21956
PMID:26833949
Abstract

Effects of exposure of 4 h to mobile phones microwaves at 1765 MHz at a power density around 940 mW/m(2) on four typical proteins (hemoglobin in H2 O solution, and myoglobin, bovine serum albumin, and lysozyme in D2 O solution) were studied by means of Fourier Transform Infrared spectroscopy and Fourier self-deconvolution analysis. Increase in intensity of parallel β-sheet component around 1635 cm(-1) was observed after exposure of hemoglobin, myoglobin, and bovine serum albumin, showing that a mechanism of unfolding occurred after exposure, whereas no appreciable change in the amide I region occurred after lysozyme exposure. In addition, a relationship between protein dipole moment and protein unfolding rate was demonstrated with a correlation coefficient r = 0.973 and 95% confidence interval.

摘要

通过傅里叶变换红外光谱和傅里叶自去卷积分析,研究了在功率密度约为940 mW/m²、频率为1765 MHz的条件下,暴露于手机微波4小时对四种典型蛋白质(H₂O溶液中的血红蛋白、D₂O溶液中的肌红蛋白、牛血清白蛋白和溶菌酶)的影响。暴露后,观察到血红蛋白、肌红蛋白和牛血清白蛋白在1635 cm⁻¹左右的平行β-折叠成分强度增加,表明暴露后发生了蛋白质展开机制,而溶菌酶暴露后酰胺I区域没有明显变化。此外,还证明了蛋白质偶极矩与蛋白质展开速率之间的关系,相关系数r = 0.973,置信区间为95%。

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