Chaperonin-mediated protein folding at the surface of groEL through a 'molten 
globule'-like intermediate

Martin, J.; Langer, T.; Boteva, R.; Schramel, A.; Horwich, A. L.; Hartl, F. U.

doi:10.1038/352036a0

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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., & Hartl, F. U. (1991). Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature, 352(6330), 36-42. doi:10.1038/352036a0.

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Item Permalink: https://hdl.handle.net/21.11116/0000-000B-6FA4-0 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-6FA5-F

Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/1676490 (Any fulltext) Open Access status unknown

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Martin, J., Author
Langer, T.¹, Author
Boteva, R., Author
Schramel, A., Author
Horwich, A. L., Author
Hartl, F. U., Author

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1Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society, ou_3393994

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Free keywords: Adenosine Triphosphate/metabolism Bacterial Proteins/*pharmacology Chaperonin 60 Heat-Shock Proteins/*pharmacology Hydrolysis Protein Conformation/*drug effects Tetrahydrofolate Dehydrogenase/chemistry Thiosulfate Sulfurtransferase/chemistry

Abstract: Folding of two monomeric enzymes mediated by groE has been reconstituted in vitro. The groEL protein stabilizes the polypeptides in a conformation resembling the 'molten globule' state. Mg-ATP and groES then promote the acquisition of ordered tertiary structure at the surface of groEL. Folding requires the hydrolysis of about 100 ATP molecules per protein monomer. This active process of surface-mediated chain folding might represent a general mechanism for the formation of protein structure in vivo.

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Dates: Published Online: 1991-07-04Date issued: 1991-07-04

Publication Status: Issued

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Identifiers: Other: 1676490
DOI: 10.1038/352036a0
ISSN: 0028-0836 (Print)0028-0836 (Linking)

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Title: Nature

Source Genre: Journal

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Pages: - Volume / Issue: 352 (6330) Sequence Number: - Start / End Page: 36 - 42 Identifier: -