Microwave-enhanced folding and denaturation of globular proteins.
It is shown that microwave irradiation can affect the kinetics of the folding process of some globular proteins, especially beta-lactoglobulin. At low temperature the folding from the cold denatured phase of the protein is enhanced, while at a higher temperature the denaturation of the protein from its folded state is enhanced. In the latter case, a negative temperature gradient is needed for the denaturation process, suggesting that the effects of the microwaves are nonthermal. This supports the notion that coherent topological excitations can exist in proteins. The application of microwaves hold promises for a wide range of biotechnological applications, such as protein synthesis, protein aggregation, etc., and may have implications for biological systems as well.
Bohr
H
H
Institute of Physics, Building 307, The Technical University of Denmark, DK-2800 Lyngby, Denmark.
Bohr
J
J
D055592:Biophysical Phenomena; D001703:Biophysics; D066298:In Vitro Techniques; D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry; D008872:Microwaves; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D007782:Lactoglobulins; D011506:Proteins