ArticleChemical communications (Cambridge, England)2025
Sigmatropic rearrangement enables access to a highly stable spirocyclic nitroxide for protein spin labelling.
Article in Chemical communications (Cambridge, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Recent advances in quantifying protein conformational ensembles with dipolar EPR spectroscopy.Current opinion in structural biology · 2025Review
- Sigmatropic rearrangement enables access to a highly stable spirocyclic nitroxide for protein spin labelling.Chemical communications (Cambridge, England) · 2025Article
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Authors and funding
7 authors.
Funding
Abstract
Spin labelling enables the study of biomolecules using electron paramagnetic resonance (EPR) spectroscopy. Here, we describe the synthesis of a cysteine-reactive spin label based on a spirocyclic pyrrolidinyl nitroxide containing an iodoacetamide moiety. The spin label was shown to be highly persistent under reducing conditions while maintaining excellent EPR relaxation parameters up to a temperature of 180 K. After successful double spin labelling of a calmodulin variant, interspin distances were measured by the EPR experiment double electron-electron resonance (DEER) at 120 K.
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Registered trials
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