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

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

Document Type: Review Article


Affiliations: Palladin Institute of Biochemistry, 9, Leontovich st., Kiev 01030, Ukraine. , Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology, 45, Vasylkivska st., Kiev 03022, Ukraine.

Publication date: 2004-02-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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