Exposure to microwave radiation enhances the aggregation of bovine serum albumin in vitro in a time-and temperature-dependent manner. Microwave radiation also promotes amyloid ¢bril formation by bovine insulin at 60 ‡C. These alterations in protein conformation are not accompanied by measurable temperature changes, consistent with estimates from ¢eld modelling of the speci¢c absorbed radiation (15^20 mW kg 31 ). Limited denaturation of cellular proteins could explain our previous observation that modest heat-shock responses are induced by microwave exposure in Caenorhabditis elegans. We also show that heat-shock responses both to heat and microwaves are suppressed after RNA interference ablating heat-shock factor function. ß

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A note on versions:The version presented here may differ from the published version or from the version of record. If you wish to cite this item you are advised to consult the publisher's version. Please see the repository url above for details on accessing the published version and note that access may require a subscription. suggestions that RF power is dissipated mainly in the plasma membrane of cells. However, these phenotype shifts are no longer seen when microwave treatment is applied at 21C in a modified exposure apparatus that minimises the temperature difference between sham and exposed conditions. Like other biological effects attributed to microwaves in the C. elegans system, phenotype shifts in ts mutants appear to be an artefact caused by very slight heating.