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Article

Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.

The Journal of biological chemistry - 17 Jun 2011

Iwasa Hisanori, Meshitsuka Shunsuke, Hongo Kunihiro, Mizobata Tomohiro, Kawata Yasushi

Abstract excerpt

Co-chaperonin GroES from Escherichia coli works with chaperonin GroEL to mediate the folding reactions of various proteins. However, under specific conditions, i.e. the completely disordered state in guanidine hydrochloride, this molecular chaperone forms amyloid fibrils similar to those observed in various neurodegenerative diseases. Thus, this is a good model system to understand the amyloid fibril formation...

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Identifiers

PMID: 21507961
DOI: 10.1074/jbc.M111.228445
PMCID: PMC3122234

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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