ArticleChemphyschem : a European journal of chemical physics and physical chemistry2011
Long-lived states to monitor protein unfolding by proton NMR.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 45 citations in OpenAlex.
- Long-lived coherences for the observation of oxidation kinetics on different timescales by NMR.Communications chemistry · 2026Article
- Improved detection of magnetic interactions in proteins based on long-lived coherences.Communications chemistry · 2024Article
- Article
- Early Divergence in Misfolding Pathways of Amyloid-Beta Peptides.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
- Singlet-filtered NMR spectroscopy.Science advances · 2020Article
- Nuclear singlet multimers (NUSIMERs) with long-lived singlet states.Chemical science · 2019Article
- SABRE-Relay: A Versatile Route to Hyperpolarization.The journal of physical chemistry letters · 2018Article
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
Abstract
The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to obtain information about partial unfolding of proteins. We detected the appearance of a destabilized conformer of ubiquitin when urea is added to the protein in its native state. This conformer shows increased mobility in the C-terminus, which significantly extends the lifetimes of proton LLS magnetisation in Ser-65. These changes could not be detected by conventional measurements of T(1) and T(2) relaxation times of protons, and would hardly be sensed by carbon-13 or nitrogen-15 relaxation measurements. Conformers with similar dynamic and structural features, as revealed by LLS relaxation times, could be observed, in the absence of urea, in two ubiquitin mutants, L67S and L69S.
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Registered trials
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