The protein was exposed to microwaves only, conventional heat (water bath) only and combinations of heat and microwaves.
Unfolding proteins tend to bind to chaperones on their unfolding pathway and this attachment is monitored by surface plasmon resonance.
|Exposure duration||continuous for 10, 15, and 20 s|
|Chamber||A shelf made from high density polyethylene with holes fitting the Eppendorf tubes was located in the microwave oven cavity with a water ballast placed under it in a fixed spot in order to stabilise the field.|
|Setup||The protein solution in an Eppendorf tube of 80 µl volume was placed in the hole determined to have the maximum temperature rise.|
|Additional info||The temperature rise near the end-tip of the Eppendorf tube was measured over a volume of 0.8 mm side length using a fluoroptic probe.|
The data showed that microwaves caused a significantly higher degree of unfolding than conventional thermal stress for protein solutions heated to the same maximum temperature. The data support the hypothesis that microwaves have a non-thermal effect on protein conformation that could take the form of a direct interaction of the electromagnetic field with the protein or its water of hydration.