Are the conformational dynamics and the ligand binding properties of myoglobin affected by exposure to microwave radiation?
| Autor: | Ettore Bismuto, Rita Massa, Fabrizio Mancinelli, G. d'Ambrosio |
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| Přispěvatelé: | Bismuto, E., Mancinelli, F., D'Ambrosio, Guglielmo, Massa, R. |
| Rok vydání: | 2003 |
| Předmět: |
Circular dichroism
Absorption spectroscopy Macromolecular Substances Protein Conformation Biophysics Radiation Dosage chemistry.chemical_compound Motion Animals Microwaves chemistry.chemical_classification Chemistry Myoglobin Tuna Biomolecule Circular Dichroism Myocardium Specific absorption rate Dose-Response Relationship Radiation General Medicine Carbon Dioxide Crystallography Spectrometry Fluorescence Non-thermal microwave effect Microwave Macromolecule Protein Binding |
| Popis: | The global uptake of mobile communication emphasizes the question about possible adverse consequences of the exposure to low-level radiofrequency radiation from mobile phones on human health as result of so-called "non-thermal effects". In order to state safety guidelines it seems appropriate to start by excluding, if possible, non-specific effects on structural and dynamic properties of fundamental biomolecules such as proteins. Proteins are flexible polyelectrolytes; thus, they are susceptible, in principle, to the action of electromagnetic fields. In this article, we investigated the effects of microwaves on structural and functional properties of Tunnus tynnus myoglobin at 1.95 GHz, a frequency used by new wireless microwave communication systems. The protein solution was exposed for 2.5 h to 51 mW/g SAR (specific absorption rate) level. Measurements of absorption spectroscopy, circular dichroism and fluorescence emission decay in the frequency domain do not exhibit any influence of the radiation on the native structural state of protein macromolecules. |
| Databáze: | OpenAIRE |
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