ArticleAngewandte Chemie (International ed. in English)2016
(19)F Paramagnetic Relaxation Enhancement: A Valuable Tool for Distance Measurements in Proteins.
Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
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- Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026Article
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- 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
- Molecular mechanism by which SARS-CoV-2 Orf9b suppresses the Tom70-Hsp90 interaction to evade innate immunity.bioRxiv : the preprint server for biology · 2025Article
- Revealing the Nature of Non-Covalent Interactions in Ionic Liquids by Combined Pulse EPR andAngewandte Chemie (International ed. in English) · 2025Article
- Decoherence of Hyperfine CoupledThe journal of physical chemistry. B · 2025Article
- Monitoring conformational changes in the human neurotransmitter transporter homologue LeuT withJournal of neurochemistry · 2025Article
- Perspectives on Applications ofMolecules (Basel, Switzerland) · 2024Review
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- Decorating phenylalanine side-chains with triple labeledJournal of biomolecular NMR · 2024Article
- 2'-Frontiers in molecular biosciences · 2024Article
- Selective polypeptide ligand binding to the extracellular surface of the transmembrane domains of the class B GPCRs GLP-1R and GCGR.iScience · 2023Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
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Abstract
Fluorine NMR paramagnetic relaxation enhancement was evaluated as a versatile approach for extracting distance information in selectively F-labeled proteins. Proof of concept and initial applications are presented for the HIV-inactivating lectin cyanovirin-N. Single F atoms were introduced at the 4-, 5-, 6- or 7 positions of Trp49 and the 4-position of Phe4, Phe54, and Phe80. The paramagnetic nitroxide spin label was attached to Cys residues that were placed into the protein at positions 50 or 52. (19)F-T2 NMR spectra with different relaxation delays were recorded and the transverse (19)F-PRE rate, (19)F-Γ2 , was used to determine the average distance between the F nucleus and the paramagnetic center. Our data show that experimental (19)F PRE-based distances correspond to 0.93 of the (1)HN-PRE distances, in perfect agreement with the gyromagnetic γ(19)F/γ(1)H ratio, thereby demonstrating that (19)F PREs are excellent alternative parameters for quantitative distance measurements in selectively F-labeled proteins.
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