Microwave enhanced kinetics observed in ORD studies of a protein.
Microwaves are shown to affect the kinetics of conformational changes of the protein beta-lactoglobulin. Microwaves can accelerate conformational changes in the direction towards the equilibrium state. This applies both for the folding and the unfolding processes. Cold denaturing thermal unfolding of the proteins is accelerated by negative temperature gradients. Microwave irradiation of the protein solution heated it by about 0.3 degree, and hence the observed acceleration of denaturing is therefore non-thermal.
Bohr
H
H
Department of Physics, Building 307, The Technical University of Denmark, Lyngby, Denmark.
Bohr
J
J
D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry / Q000528:radiation effects*; D008872:Microwaves; D009905:Optical Rotatory Dispersion / Q000379:methods; D011487:Protein Conformation / Q000528:radiation effects*; D011489:Protein Denaturation; D014508:Urea
D007782:Lactoglobulins; D014508:Urea