ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025
Deep Learning for Hyperpolarized NMR of Intrinsically Disordered Proteins without Resolution Loss: Access to Short-Lived Intermediates.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Article
- Residue-Specific Signatures of Structural Water Identified by Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.Angewandte Chemie (International ed. in English) · 2026Article
- Hyperpolarized NMR Reveals Low-Populated Folding Intermediates in DNA.Journal of the American Chemical Society · 2025Article
- Enhancing NMR Signals in Liquids by Fluorine-19 Overhauser Dynamic Nuclear Polarization (DNP) and Hyperpolarization Transfer to Carbon-13.Angewandte Chemie (International ed. in English) · 2025Article
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6 authors.
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Abstract
The inherently low sensitivity of solution-state Nuclear Magnetic Resonance (NMR) has long limited its ability to characterize transient biomolecular states at atomic resolution. While dissolution dynamic nuclear polarization (dDNP) offers a compensating signal enhancement, its broader use has been hindered by rapid polarization decay, causing severe spectral distortion. Here, we introduce HyperW-Decon, an approach that enables high-sensitivity, high-resolution NMR of biomolecules in solution. HyperW-Decon combines two key aspects: (i) the use of hyperpolarized water (HyperW) to transfer polarization to proteins through rapid proton exchange; and (ii) a theory-driven, machine learning (ML)-based deconvolution method that corrects polarization-induced artifacts without requiring external reference signals. This approach is based on a first-principles understanding of dDNP line shapes and delivers a scalable solution to spectral distortion. Applied to intrinsically disordered proteins (IDPs) involved in biomineralization, HyperW-Decon reveals previously inaccessible, short-lived ion-peptide encounter complexes with residue resolution.
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