Biophysical studies on the molecular chaperone function, structure and interaction of eye lens protein α-crystallin - A Review

Ashis Biswas, Srabani Karmakar, Victor Banerjee, Sudipa Saha, Madhuchhanda Kundu, Jaya Bhattacharyya, Dipak Chandra Konar, K. P. Das

Research output: Contribution to journalReview articlepeer-review


α-Crystallin is the major constituent protein of the eye lens of the vertebrates. It is an oligomeric protein having micelle like architecture. Ever since it was reported in early 90's that it possesses molecular chaperone like function which is crucial for the maintenance of the transparency of the eye lens, interests in understanding the mechanism of such function developed rapidly. Various laboratories have contributed towards understanding of the structure and function of this protein. Our group has been engaged to study specific problems related to this area. We undertook detailed study to understand the structure of bound substrates employing a combination of simple molecular biology and biophysical tools to show that α-crystallin recognizes early folding intermediates and bound substrates have native-like structure. Our work showed that chaperone activity correlated fairly well with exposed surface hydrophobicity. We proved that temperature activation was not required for α-crystallin to function as chaperone as was proposed by others. Very importantly we demonstrated that some small molecules such as ATP can interact with α-crystallin to form weak associated chaperone-substrate complex that can play crucial role in increasing the thermodynamic stability and chaperone function and refractive properties of the lens. Some bivalent metal ions such as Zn2+ plays a very important role in the structure, stability and chaperone function of α-crystallin and such a sore has considerable physiological significance in understanding the cataract formation in the lens. This article is not intended to be a comprehensive account of all aspects of work done on this protein. But instead in this article we have reviewed primarily our work and mentioned the work done by others in these specific areas only.

Original languageEnglish
Pages (from-to)1827-1855
Number of pages29
JournalJournal of the Indian Chemical Society
Issue number12
StatePublished - 1 Jan 2011
Externally publishedYes


  • Binding sites
  • Eye lens protein
  • Hydrophobicity
  • Molecular chaperone
  • Protein-ptotein interaction
  • Structural recognition
  • Subunit exchange
  • Thermal aggregation
  • α-Crystallin

ASJC Scopus subject areas

  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry
  • Electrochemistry


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