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Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein

Chaperonin GroEL from Escherichia coli consists of two heptameric rings stacked back-to-back to form a cagelike structure. It assists in the folding of substrate proteins in concert with the co-chaperonin GroES by incorporating them into its large cavity. The mechanism underlying the incorporation o...

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Detalhes bibliográficos
Publicado no:J Biol Chem
Main Authors: Ishino, So, Kawata, Yasushi, Taguchi, Hideki, Kajimura, Naoko, Matsuzaki, Katsumi, Hoshino, Masaru
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2015
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4463448/
https://ncbi.nlm.nih.gov/pubmed/25887400
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M114.633636
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