Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study.

@article{Galan2001ExcludedVE,
  title={Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study.},
  author={A. Cerezo Galan and Bego{\~n}a Sot and Oscar Llorca and Jos{\'e} L Carrascosa and Jos{\'e} Mar{\'i}a Valpuesta and Arturo Muga},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 2},
  pages={957-64}
}
We have studied the effect of macromolecular crowding reagents, such as polysaccharides and bovine serum albumin, on the refolding of tetradecameric GroEL from urea-denatured protein monomers. The results show that productive refolding and assembly strongly depends on the presence of nucleotides (ATP or ADP) and background macromolecules. Nucleotides are required to generate an assembly-competent monomeric conformation, suggesting that proper folding of the equatorial domain of the protein… CONTINUE READING

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