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EMF Study
(Database last updated on Mar 27, 2024)
ID Number |
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2111 |
Study Type |
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Engineering & Physics |
Model |
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Modeling of microwave exposure to various molecules and proteins (egg white lysozyme) and analysis of denaturization and refolding kinetics. |
Details |
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Simulations were performed on denatured hen egg white lysozyme protein to evaluate denaturization - refolding kinetics in the presence of microwave and far-infrared electromagnetic waves. The authors report accelerated local denaturation and significant changes in protein secondary structure due to non-thermal interactions with microwaves and far-infrared due to changes in the alignment of protein dipole moment. In a related study, the authors modeled the effects of microwave and far-infrared frequencies on binary mixtures of dimethylimidazolium hexafluorophosphate salts and water and again observed changes in dipole alignment and molecular mobility under non-thermal conditions.
AUTHORS' ABSTRACT: Solomentsev, English and Mooney 2010 (IEEE #6286): Nonequilibrium molecular dynamics simulations of a charge-neutral mutant of hen egg white lysozyme have been performed at 300 K and 1 bar in the presence of external microwave fields (2.45 to 100 GHz) of an rms electric field intensity of 0.05 V Å(-1). A systematic study was carried out of the distributions of persistence times and energies of each intraprotein hydrogen bond in between breakage and reformation, in addition to overall persistence over 20 ns simulations, vis-á-vis equilibrium, zero-field conditions. It was found that localized translational motion for formally charged residues led to greater disruption of associated hydrogen bonds, although induced rotational motion of strongly dipolar residues also led to a degree of hydrogen bond perturbation. These effects were most apparent in the solvent exposed exterior of hen egg white lysozyme, in which the intraprotein hydrogen bonds tend to be weaker. |
Findings |
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Effects |
Status |
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Completed With Publication |
Principal Investigator |
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University College Dublin, Ireland - niall.english@ucd.ie
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Funding Agency |
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?????
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Country |
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IRELAND |
References |
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English, NJ et al. Phys Chem Chem Phys, (2009) 11:9370-9374
English, NJ et al. J Phys Chem B, (2009) 113:10128-10134
English, NJ et al. J Chem Phys, (2007) 126:091105-091109
Solomentsev, GY et al. J Chem Phys., (2010) 133(23):235102-
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