ID Number		1739
Study Type		Engineering & Physics
Model		Theoretical modeling of protein conformational changes due to RF exposure
Details		Theoretical modeling (using a Nanoscale Molecular Dynamics computer program) of insulin under exposure to 1.25, 2.45, and 4.9 GHz RF. Specific focus was placed on the alpha-helix of the insulin B-chain. Protein simulations were performed using equilibrium conditions, chemical stress (reducing disulfide bonds), or intermittent (2 ns) thermal stress. The authors report that at high field stringths, the lower (1.225 GHz) frequency interacted stronger with the helical structure of insulin inhibbitting the active state, while the higher frequency (4.9 GHz) induced more instantaneous destabilization. RF also increased the water contact area and decreased the solvent accessible surface area. The effects of very short (2 ns) temperature elevations are likely the mechanism behind the RF induced changes. A combination of thermal and chemical stresses seemed to result in the greatest conformational changes.
Findings		Not Applicable to Bioeffects
Status		Completed With Publication
Principal Investigator		RMIT University, Melborurne Australia - irene.yarovsky@rmit.edu.au
Funding Agency		NHMRC, Australia
Country		AUSTRALIA
References		Budi, et al. Eur Biophys J Biophys Lett, (2004) 33:121-129 Budi, A et al. J Phys Chem Biol, (2007) 111:5748-5756 Noble, BB et al. Phys Chem Chem Phys., (2022) 24:6327-6348
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