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Abstract

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.

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PubMed ID:: 10532860

DOI:: 10.1038/342884a0

ScienceOpen disciplines: Chemistry

Keywords: Adenosine Triphosphate,metabolism,Chaperonin 10,Chaperonin 60,Chloroplasts,enzymology,Escherichia coli,Protein Conformation,Ribulose-Bisphosphate Carboxylase,chemistry

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ScienceOpen disciplines: Chemistry

Keywords: Adenosine Triphosphate, metabolism, Chaperonin 10, Chaperonin 60, Chloroplasts, enzymology, Escherichia coli, Protein Conformation, Ribulose-Bisphosphate Carboxylase, chemistry

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