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Molecular chaperones: Inside a nd outside the Anfinsen cage
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UNSPECIFIED (2001) Molecular chaperones: Inside a nd outside the Anfinsen cage. CURRENT BIOLOGY, 11 (24). R1038-R1040. ISSN 0960-9822.
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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.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | CURRENT BIOLOGY | ||||
Publisher: | CELL PRESS | ||||
ISSN: | 0960-9822 | ||||
Official Date: | 11 December 2001 | ||||
Dates: |
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Volume: | 11 | ||||
Number: | 24 | ||||
Number of Pages: | 3 | ||||
Page Range: | R1038-R1040 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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