Macromolecular crowding extended to a heptameric system: the Co-chaperonin protein 10.

@article{Aguilar2011MacromolecularCE,
  title={Macromolecular crowding extended to a heptameric system: the Co-chaperonin protein 10.},
  author={Ximena Aguilar and Christoph F Weise and T Sparrman and Magnus Wolf-Watz and Pernilla Wittung-Stafshede},
  journal={Biochemistry},
  year={2011},
  volume={50 14},
  pages={3034-44}
}
Experiments on monomeric proteins have shown that macromolecular crowding can stabilize toward heat perturbation and also modulate native-state structure. To assess the effects of macromolecular crowding on unfolding of an oligomeric protein, we here tested the effects of the synthetic crowding agent Ficoll 70 on human cpn10 (GroES in E. coli), a heptameric protein consisting of seven identical β-barrel subunits assembling into a ring. Using far-UV circular dichroism (CD), tyrosine fluorescence… CONTINUE READING

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