Article citationsMore>>

Kokke, B.P.A., Leroux, M.R., Candido, E.P.M., Boelens, W.C. and de Jong, W.W. (1998) Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity. FEBS Letters, 433, 228-232.
http://dx.doi.org/10.1016/S0014-5793(98)00917-X

has been cited by the following article:

• TITLE: Structure and interactions in α-crystallin probed through thiol group reactivity

  AUTHORS: Sudipa Saha, Kali Pada Das

  KEYWORDS: Thiol Reactivity; α-Crystallin; DTNB Kinetics; Molecular Chaperone; Folding Unfolding of α-Crystallin

  JOURNAL NAME: Advances in Biological Chemistry, Vol.3 No.5, February 21, 2014

  ABSTRACT: a-Crystallin is the major structural protein of eye lens of vertebrates. In human lens, the ratio of aA-crystallin to aB-crystallin was found to be 3:1. aA-Crystallin contains two cysteine residues at positions 131 and 142, which are at the junction between the a-crystallin domain and the C-terminal tail. We used the accessibility of the thiol groups by Ellman’s reagent (DTNB) as a tool to gain information about the various structural perturbations of hinge region of a-crystallin and during the binding with substrates. In the native condition, the cys-142 though reacted quite fast was not fully exposed. Several reagents were used to see the accessibility of cys-131. Rate constant for cys-131 was increased gradually with increase in the concentration of reagents. The bindings of substrates are affected by the accessibility of thiol indicating that the substrates bind to the hinge region of a-crystallin. By blocking of cys-142, it was observed that the accessibility of one thiol depends on the other thiol, and they are not independent. The hinge region of a-crystallin is very important as substrate binding site and from this study we have got various structural information about that region.