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Article

Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.

Cell - 2 Jun 2006

Tang Yun-Chi, Chang Hung-Chun, Roeben Annette, Wischnewski Dirk, Wischnewski Nadine, Kerner Michael J, Hartl F Ulrich, Hayer-Hartl Manajit

Abstract excerpt

GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (approximately 30 kDa) folded more rapidly as the size of the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16751100
DOI: 10.1016/j.cell.2006.04.027

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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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