期刊
CURRENT BIOLOGY
卷 11, 期 24, 页码 R1038-R1040出版社
CELL PRESS
DOI: 10.1016/S0960-9822(01)00620-0
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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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