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Article

A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.

Journal of molecular biology - 14 May 2004

Poso Daniel, Clarke Anthony R, Burston Steven G

Abstract excerpt

The function of GroE requires a complex system of allosteric communication driven by protein-nucleotide interactions. These rearrangements couple the binding and hydrolysis of ATP to an overall reaction cycle in which substrate proteins are bound, encapsulated and released. Positive cooperativity with respect to ATP binding occurs within one heptameric ring of GroEL, while negative cooperativity between the two...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15111060
DOI: 10.1016/j.jmb.2004.03.010

Provenance

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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A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.PMID 15111060Read ↗

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