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Article

Flexible interwoven termini determine the thermal stability of thermosomes.

Protein & cell - 1 Jun 2013

Zhang Kai, Wang Li, Liu Yanxin, Chan Kwok-Yan, Pang Xiaoyun, Schulten Klaus, Dong Zhiyang, Sun Fei

Abstract excerpt

Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and...

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Identifiers

PMID: 23709365
DOI: 10.1007/s13238-013-3026-9
PMCID: PMC3740188

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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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