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Article

Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.

The journal of physical chemistry. B - 29 Dec 2005

Kim So Yeon, Semyonov Alexander N, Twieg Robert J, Horwich Arthur L, Frydman Judith, Moerner W E

Abstract excerpt

Hydrophobic interactions play a major role in binding non-native substrate proteins in the central cavity of the bacterial chaperonin GroEL. The sequence of local conformational changes by which GroEL and its cofactor GroES assist protein folding can be explored using the polarity-sensitive fluorescence probe Nile Red. A specific single-cysteine mutant of GroEL (Cys261), whose cysteine is located inside the...

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Identifiers

PMID: 16375456
DOI: 10.1021/jp0534232
PMCID: PMC1414071

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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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