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
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	CURRENT BIOLOGY
Publisher:	CELL PRESS
ISSN:	0960-9822
Date:	11 December 2001
Volume:	11
Number:	24
Number of Pages:	3
Page Range:	R1038-R1040
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/11406

Data sourced from Thomson Reuters' Web of Knowledge

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