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Updated: Aug 14, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
[Effect of hydrostatic pressure on quaternary structure on the chaperone function of alpha-crystallin]
S Avilov1, Ch Bode, F Told'oshr
1Palladin Institute of Biochemistry of NAS of Ukraine, Kyiv.
Abstract:
High hydrostatic pressure-induced changes in bovine lens alpha-crystallin oligomers size and chaperone-like function were studied by a static light scattering. Under pressure 1.5 kbar, alpha-crystallin oligomers size is almost unaffected. Increase of the size was observed during several hours of incubation at 3 kbar. Such high-pressure effect on association has been previously revealed for detergent micelles, whereas the "typical" protein oligomers are known to dissociate under high pressure. Our results about pressure influence on alpha-crystallin association supports the previously proposed "protein micelle" model of the protein quaternary structure. Chaperone-like activity of alpha-crystallin is shown to increase after incubation at 3 kbar. After the end of the incubation this activity is slowly decreasing during several hours.
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