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

Sergiy V. Avilov; Nataliya A. Aleksandrova; Alexander P. Demchenko

doi:10.2174/0929866043478437

ISSN: 0929-8665
E-ISSN: 1875-5305

Quaternary Structure Of α-Crystallin Is Necessary For The Binding Of Unfolded Proteins: A Surface Plasmon Resonance Study
Authors: Sergiy V. Avilov¹, Nataliya A. Aleksandrova² and Alexander P. Demchenko³
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¹ Palladin Institute of Biochemistry, 9, Leontovich st., Kiev 01030, Ukraine. , Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology, 45, Vasylkivska st., Kiev 03022, Ukraine. ² Palladin Institute of Biochemistry, 9, Leontovich st., Kiev 01030, Ukraine. , Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology, 45, Vasylkivska st., Kiev 03022, Ukraine. ³ Palladin Institute of Biochemistry, 9, Leontovich st., Kiev 01030, Ukraine. , Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology, 45, Vasylkivska st., Kiev 03022, Ukraine.
Source: Protein and Peptide Letters, Volume 11, Issue 1, Feb 2004, p. 41 - 48
DOI: https://doi.org/10.2174/0929866043478437
- Available online: 01 Feb 2004

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.

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2004-02-01

2025-09-18

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Article Type: Review Article

Keyword(s): chaperone-like activity; crystallin; small heat shock protein; surface plasmon resonance

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

Abstract

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