Molecular chaperones: Inside and outside the Anfinsen cage
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چکیده
منابع مشابه
Molecular chaperones: Inside and outside the Anfinsen cage
The GroEL/GroES chaperonin system acts as a passive anti-aggregation cage for refolding rubisco and rhodanese, and not as an active unfolding device. Refolding aconitase is too large to enter the cage but reversible binding to GroEL reduces its aggregration. Unexpectedly, confinement in the cage increases the rate of refolding of rubisco, but not rhodanese.
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Although we have a rather elaborate "working-cycle" for the 60 kDa molecular chaperones, which possess a cavity, and are called Anfinsen-cage-type chaperones to emphasize that they provide a closed, protected environment to help the folding of their substrates, our understanding of the molecular mechanism of how these chaperones help protein folding is still incomplete. The present study adds t...
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ژورنال
عنوان ژورنال: Current Biology
سال: 2001
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(01)00620-0