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Article

Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.

Journal of molecular biology - 29 Jul 2014

Gupta Amit J, Haldar Shubhasis, Miličić Goran, Hartl F Ulrich, Hayer-Hartl Manajit

Abstract excerpt

The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coli have an essential role in assisting protein folding by transiently encapsulating non-native substrate in an ATP-regulated mechanism. It remains controversial whether the chaperonin system functions solely as an infinite dilution chamber, preventing off-pathway aggregation, or actively enhances folding kinetics by modulating the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 24816391
DOI: 10.1016/j.jmb.2014.04.018

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MBP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.PMID 24816391Read ↗

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The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain.Semantic proximity Read ↗

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