Open AccessA thermal after-effect of UV irradiation of muscle glycogen phosphorylase b
Author(s) -
Valeriya V. Mikhaylova,
Tatiana B. Eronina,
Natalia A. Chebotareva,
Sergey Y. Kleymenov,
Vladimir Shubin,
B. I. Kurganov
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0189125
Subject(s) - glycogen phosphorylase , glycogen , biophysics , irradiation , chemistry , protein aggregation , kinetics , chaperone (clinical) , biochemistry , limiting , protein folding , biology , medicine , mechanical engineering , physics , pathology , quantum mechanics , nuclear physics , engineering
Different test systems are used to characterize the anti-aggregation efficiency of molecular chaperone proteins and of low-molecular-weight chemical chaperones. Test systems based on aggregation of UV-irradiated protein are of special interest because they allow studying the protective action of different agents at physiological temperatures. The kinetics of UV-irradiated glycogen phosphorylase b (UV-Ph b ) from rabbit skeletal muscle was studied at 37°C using dynamic light scattering in a wide range of protein concentrations. It has been shown that the order of aggregation with respect to the protein is equal to unity. A conclusion has been made that the rate-limiting stage of the overall process of aggregation is heat-induced structural reorganization of a UV-Ph b molecule, which contains concealed damage.