Microwave-enhanced folding and denaturation of globular proteins

It is shown that microwave irradiation can affect the kinetics of the foldi ng process of some globular proteins, especially beta-lactoglobulin. At low temperature the folding from the cold denatured phase of the protein is en hanced, while at a higher temperature the denaturation of the protein from its folded state is enhanced. In the latter case, a negative temperature gr adient is needed for the denaturation process, suggesting that the effects of the microwaves are nonthermal. This supports the notion that coherent to pological excitations can exist in proteins. The application of microwaves hold promises for a wide range of biotechnological applications, such as pr otein synthesis, protein aggregation, etc., and may have implications for b iological systems as well.