ArticlePhysical chemistry chemical physics : PCCP2026
NMR-based conformational analysis of DNA G-quadruplex guides mapping essential structure-function relationship in protein chaperoning.
Article in Physical chemistry chemical physics : PCCP, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed.
- Structural basis of chaperone mechanisms in cells and the evolutionary emergence of the protein world.bioRxiv : the preprint server for biology · 2026Article
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5 authors.
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Abstract
G-quadruplexes (G4s) are increasingly recognized to chaperone proteins, warranting studies of structure-function relationships. In this study, we apply solution NMR methods to determine the topology and base-level resolution structure of a G-rich DNA sequence with protein chaperoning activity (referred to as Seq576) without chemical shift assignments. Seq576 samples two conformations, in the slow exchange timescale, arising from a G-register shift. Using the structural insights of Seq576, we then perform structure-function studies
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