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Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL

The chaperonin GroEL binds nonnative proteins in its central channel through hydrophobic interactions and initiates productive folding in this space underneath bound cochaperone, GroES, in the presence of ATP. The questions of where along the folding pathway a protein is recognized by GroEL, and how...

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Autori principali: Goldberg, Matthew S., Zhang, Jing, Sondek, Stacey, Matthews, C. Robert, Fox, Robert O., Horwich, Arthur L.
Natura: Artigo
Lingua:Inglês
Pubblicazione: The National Academy of Sciences of the USA 1997
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC19747/
https://ncbi.nlm.nih.gov/pubmed/9037009
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