Microwave radiation can alter protein conformation without bulk heating

Abstract

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 fibril formation by bovine insulin at 60°C. These alterations in protein conformation are not accompanied by measurable temperature changes, consistent with estimates from field modelling of the specific absorbed radiation (15–20 mW kg −1 ). 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.