ID Number		529
Study Type		In Vitro
Model		2450 MHz (CW) exposure to purified beta-lactoglobulin protein and analysis of structure and folding
Details		Purified beta-lactoglobulin protein was denatured in urea, cooled to 4 degrees, and renatured by increasing the temperature by 2 degree increments until renaturization was observed (as seen spectrophotmetrically). Exposure to 2450 MHz (CW) accelerated both the denaturization and renaturization process. Since the solution was only observed to increase in temperature by 0.3 degrees as a result of the 2450 MHz exposure, the authors suggest this reports a non-thermal effect.
Findings		Effects
Status		Completed With Publication
Principal Investigator		The Technical University of Denmark
Funding Agency		Private/Instit.
Country		DENMARK
References		Bohr, H et al. Physical Rev, (2000) 61:4310-4314 Bohr, H et al. Bioelectromagnetics, (2000) 21:68-72 Bohr, J et al. Biophys Chem, (1997) 63:97-105 Bohr, H et al. Bioelectromagnetics., (1997) 18:187-189
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