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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 11 , Issue 1 , 2004

Page: [41 - 48] Pages: 8

DOI: 10.2174/0929866043478437

Price: $65

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.

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


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