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Article

Perturbation of the hierarchical folding of a large RNA by the destabilization of its Scaffold's tertiary structure.

Journal of molecular biology - 25 Nov 2005

Shcherbakova Inna, Brenowitz Michael

Abstract excerpt

The P4-P6 domain serves as a scaffold against which the periphery and catalytic core organize and fold during Mg2+-mediated folding of the Tetrahymena thermophila ribozyme. The most prominent structural motif of the P4-P6 domain is the tetraloop-tetraloop receptor interaction which "clamps" the distal parts of its hairpin-like structure. Destabilization of the tertiary structure of the P4-P6 domain by...

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Source

Identifiers

PMID: 16242711
DOI: 10.1016/j.jmb.2005.09.032

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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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Perturbation of the hierarchical folding of a large RNA by the destabilization of its Scaffold's tertiary structure.PMID 16242711Read ↗

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Concerted kinetic folding of a multidomain ribozyme with a disrupted loop-receptor interaction.Semantic proximity Read ↗

Folding mechanism of the Tetrahymena ribozyme P4-P6 domain.Semantic proximity Read ↗

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