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Microwave enhanced kinetics observed in ORD studies of a protein
Author(s) -
Bohr Henrik,
Bohr Jakob
Publication year - 2000
Publication title -
bioelectromagnetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.435
H-Index - 81
eISSN - 1521-186X
pISSN - 0197-8462
DOI - 10.1002/(sici)1521-186x(200001)21:1<68::aid-bem10>3.0.co;2-9
Subject(s) - kinetics , microwave , biophysics , enzyme kinetics , chemistry , biological system , physics , biology , biochemistry , enzyme , classical mechanics , quantum mechanics , active site
Microwaves are shown to affect the kinetics of conformational changes of the protein β‐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. Bioelectromagnetics 21:68–72, 2000. © 2000 Wiley‐Liss, Inc.