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Article

In vivo activities of GroEL minichaperones.

Proceedings of the National Academy of Sciences of the United States of America - 18 Aug 1998

Chatellier J, Hill F, Lund P A, Fersht A R

Abstract excerpt

Fragments encompassing the apical domain of GroEL, called minichaperones, facilitate the refolding of several proteins in vitro without requiring GroES, ATP, or the cage-like structure of multimeric GroEL. We have identified the smallest minichaperone that is active in vitro in chaperoning the refolding of rhodanese and cyclophilin A: GroEL(193-335). This finding raises the question of whether the minichaperones...

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Identifiers

PMID: 9707566
DOI: 10.1073/pnas.95.17.9861
PMCID: PMC21427

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In vivo activities of GroEL minichaperones.PMID 9707566Read ↗

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