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Review
. 2001 Dec 11;11(24):R1038-40.
doi: 10.1016/s0960-9822(01)00620-0.

Molecular chaperones: inside and outside the Anfinsen cage

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Free article
Review

Molecular chaperones: inside and outside the Anfinsen cage

R J Ellis. Curr Biol. .
Free article

Abstract

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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