Microwave-enhanced folding and denaturation of globular proteins

Henrik Bohr, Jakob Bohr

Research output: Contribution to journalJournal articleResearchpeer-review

832 Downloads (Pure)

Abstract

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.
Original languageEnglish
JournalPhysical Review E. Statistical, Nonlinear, and Soft Matter Physics
Volume61
Issue number4
Pages (from-to)4310-4314
ISSN1063-651X
DOIs
Publication statusPublished - 2000

Bibliographical note

Copyright (2000) American Physical Society

Keywords

  • OVEN

Cite this