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Article

An NMR view of the folding process of a CheY mutant at the residue level.

Structure (London, England : 1993) - 1 Sept 2002

Garcia Pascal, Serrano Luis, Rico Manuel, Bruix Marta

Abstract excerpt

The folding of CheY mutant F14N/V83T was studied at 75 residues by NMR. Fluorescence, NMR, and sedimentation equilibrium studies at different urea and protein concentrations reveal that the urea-induced unfolding of this CheY mutant includes an on-pathway molten globule-like intermediate that can associate off-pathway. The populations of native and denatured forms have been quantified from a series of 15N-1H HSQC...

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Source

Identifiers

PMID: 12220489
DOI: 10.1016/s0969-2126(02)00804-3

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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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