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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the molecular chaperones: chaperonin-60 from Escherichia coli (groEL), yeast mitochondria (hsp60) or chloroplasts (Rubisco sub-unit-binding protein), together with chaperonin-10 from E. coli (groES), and Mg-ATP. Because chaperonins are ubiquitous, a conserved Mg-ATP-dependent mechanism exists that uses the chaperonins to facilitate the folding of some other proteins.[1]

References

  1. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Goloubinoff, P., Christeller, J.T., Gatenby, A.A., Lorimer, G.H. Nature (1989) [Pubmed]
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