ArticleThe journal of physical chemistry letters2024
Quantification of Distributions of Local Proton Concentrations in Heterogeneous Soft Matter and Non-Anfinsen Biomacromolecules.
Article in The journal of physical chemistry letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Quantifying the liquid-liquid transition in cold water/glycerol mixtures by intermolecular hyperfine relaxation-induced dipolar modulation enhancement (ih-RIDME).Physical chemistry chemical physics : PCCP · 2025Article
- Revealing the Nature of Non-Covalent Interactions in Ionic Liquids by Combined Pulse EPR andAngewandte Chemie (International ed. in English) · 2025Article
- Tracking life and death of carbon nitride supports in platinum-catalyzed vinyl chloride synthesis.Nature communications · 2025Article
- RIDME Spectroscopy: New Topics Beyond the Determination of Electron Spin-Spin Distances.The journal of physical chemistry letters · 2025Review
- ih-RIDME: a pulse EPR experiment to probe the heterogeneous nuclear environment.Magnetic resonance (Gottingen, Germany) · 2025Article
- Electron-spin decoherence in trityl radicals in the absence and presence of microwave irradiation.Magnetic resonance (Gottingen, Germany) · 2025Article
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Authors and funding
8 authors.
Funding
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Abstract
A new method to quantitatively analyze heterogeneous distributions of local proton densities around paramagnetic centers in unstructured and weakly structured biomacromolecules and soft matter is introduced, and its feasibility is demonstrated on aqueous solutions of stochastically spin-labeled polysaccharides. This method is based on the pulse EPR experiment ih-RIDME (intermolecular hyperfine relaxation-induced dipolar modulation enhancement). Global analysis of a series of RIDME traces allows for a mathematically stable transformation of the time-domain data to the distribution of local proton concentrations. Two pulse sequences are proposed and tested, which combine the ih-RIDME block and the double-electron-electron resonance (DEER) experiment. Such experiments can be potentially used to correlate the local proton concentration with the macromolecular chain conformation. We anticipate an application of this approach in studies of intrinsically disordered proteins, biomolecular aggregates, and biomolecular condensates.
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Registered trials
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