期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 21, 期 6, 页码 -出版社
MDPI
DOI: 10.3390/ijms21062039
关键词
HspB6; monomeric 14-3-3 zeta; anti-aggregation activity; arginine
资金
- Russian Science Foundation [16-14-10055]
The effect of protein chaperones HspB6 and the monomeric form of the protein 14-3-3 zeta (14-3-3 zeta(m)) on a test system based on thermal aggregation of UV-irradiated glycogen phosphorylase b (UV-Phb) at 37 degrees C and a constant ionic strength (0.15 M) was studied using dynamic light scattering. A significant increase in the anti-aggregation activity of HspB6 and 14-3-3 zeta(m) was demonstrated in the presence of 0.1 M arginine (Arg). To compare the effects of these chaperones on UV-Phb aggregation, the values of initial stoichiometry of the chaperone-target protein complex (S-0) were used. The analysis of the S-0 values shows that in the presence of Arg fewer chaperone subunits are needed to completely prevent aggregation of the UV-Phb subunit. The changes in the structures of HspB6 and 14-3-3 zeta(m) induced by binding of Arg were evaluated by the fluorescence spectroscopy and differential scanning calorimetry. It was suggested that Arg caused conformational changes in chaperone molecules, which led to a decrease in the thermal stability of protein chaperones and their destabilization.
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