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Updated: Aug 26, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
Published on: November 5, 2018
Quaternary structure of alpha-crystallin is necessary for the binding of unfolded proteins: a surface plasmon
Sergiy V Avilov1, Nataliya A Aleksandrov, Alexander P Demchenko
1Palladin Institute of Biochemistry, 9, Leontovich st, Kiev 01030, Ukraine. sergavilov@gala.net
Abstract:
The interactions between an oligomeric heat-shock protein, alpha-crystallin, and its individual subunits with unfolded proteins were monitored by surface plasmon resonance. Immobilization at the sensor chip allowed us for the first time to study isolated alpha-crystallin subunits under physiological conditions. We observe that these subunits, in contrast to alpha-crystallin oligomers, do not bind unfolded protein. Our data indicate that quaternary structure of alpha-crystallin is necessary for its chaperone-like activity.
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