Skip to main content

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

Buy Article:

$63.00 plus tax (Refund Policy)

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

Document Type: Review Article

DOI: https://doi.org/10.2174/0929866043478437

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

More about this publication?
  • 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.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more