Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme.

@article{Shashidharamurthy2005MechanismOC,
  title={Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme.},
  author={R Shashidharamurthy and Hanane A. Koteiche and Jinhui Dong and Hassane S. Mchaourab},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 7},
  pages={5281-9}
}
Mammalian small heat shock proteins (sHSP) form polydisperse and dynamic oligomers that undergo equilibrium subunit exchange. Current models of their chaperone activity hypothesize that recognition and binding of protein non-native states involve changes in the oligomeric state. The equivalent thermodynamic representation is a set of three coupled equilibria that includes the sHSP oligomeric equilibrium, the substrate folding equilibrium, and the equilibrium binding between the sHSP and the… CONTINUE READING

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