Biochemistry & Analytical Biochemistry

Natalia A Chebotareva

Publications

• Editorial
  New Physiological Function of Chaperones, Facilitating Reconstitution of Apoenzymes
  Author(s): Boris I Kurganov and Natalia A ChebotarevaBoris I Kurganov and Natalia A Chebotareva
  
  One of the important branches of modern biochemistry and molecular biology is the investigation of structure and function of molecular chaperones. The main function of the family of molecular chaperones named as small heat shock proteins (sHsps) is suppression of aggregation of non-native protein species formed under stress conditions or during folding of the newly synthesized polypeptide chains [1-3]. The low molecular mass of monomers (from 12 to 43 kDa) and tendency to form large oligomers with high molecular masses up to 1000 kDa are typical of this protein family [4-14]. The presence of a conservative α-crystallin domain in the structure of sHsp seems to be important for the formation of stable dimers, whereas variable N- and C-terminal ends seem to participate in the formation of large oligomers [2-4,7]. It is supposed that the polydispersity and quaternary structure dynam.. View More»
  DOI: 10.4172/2161-1009.1000e148

  Abstract PDF