Quaternary Structure Of α-Crystallin Is Necessary For The Binding Of Unfolded Proteins: A Surface Plasmon Resonance Study

Title: Quaternary Structure Of α-Crystallin Is Necessary For The Binding Of Unfolded Proteins: A Surface Plasmon Resonance Study

Volume: 11 Issue: 1

Author(s): Sergiy V. Avilov, Nataliya A. Aleksandrova and Alexander P. Demchenko

Affiliation:

Keywords: crystallin, small heat shock protein, chaperone-like activity, surface plasmon resonance

Abstract: The interactions between an oligomeric heat-shock protein, α-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 α-crystallin subunits under physiological conditions. We observe that these subunits, in contrast to α-crystallin oligomers, do not bind unfolded protein. Our data indicate that quaternary structure of α-crystallin is necessary for its chaperone-like activity.

Cite this article as:

Avilov V. Sergiy, Aleksandrova A. Nataliya and Demchenko P. Alexander, Quaternary Structure Of α-Crystallin Is Necessary For The Binding Of Unfolded Proteins: A Surface Plasmon Resonance Study, Protein & Peptide Letters 2004; 11 (1) . https://dx.doi.org/10.2174/0929866043478437