ArticleAngewandte Chemie (International ed. in English)2020
Structure of a Protein-RNA Complex by Solid-State NMR Spectroscopy.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
- Mapping mRNA Localization and Internal Structure in Lipid Nanoparticles through Solid-State Dynamic Nuclear Polarization NMR and Proton Spin-Diffusion Modeling.Small methods · 2026Article
- Solid-state NMR of membrane peptides and proteins in the lipid cubic phase.Biophysical journal · 2025Article
- A DNP-Supported Solid-State NMR Approach to Study Nucleic Acids In Situ Reveals Berberine-Stabilized Hoogsteen Structures in Mitochondria.Angewandte Chemie (International ed. in English) · 2025Article
- Structural insights into lab-coevolved RNA-RBP pairs and applications of synthetic riboswitches in cell-free system.Nucleic acids research · 2025Article
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- RNA-protein interaction prediction using network-guided deep learning.Communications biology · 2025Article
- Elucidating microRNA-34a organisation within human Argonaute-2 by dynamic nuclear polarisation-enhanced magic angle spinning NMR.Nucleic acids research · 2024Article
- The 5'-terminal stem-loop RNA element of SARS-CoV-2 features highly dynamic structural elements that are sensitive to differences in cellular pH.Nucleic acids research · 2024Article
- Structural studies of protein-nucleic acid complexes: A brief overview of the selected techniques.Computational and structural biotechnology journal · 2023Review
- Dynamics of base pairs with low stability in RNA by solid-state nuclear magnetic resonance exchange spectroscopy.iScience · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- Characterizing hydrogen bonds in intact RNA from MS2 bacteriophage using magic angle spinning NMR.Biophysical reports · 2021Article
- Protein resonance assignment by solid-state NMR based onJournal of biomolecular NMR · 2021Article
- Identification of RNA Base Pairs and Complete Assignment of Nucleobase Resonances by Proton-Detected Solid-State NMR Spectroscopy at 100 kHz MAS.Angewandte Chemie (International ed. in English) · 2021Article
- Paramagnetic Solid-State NMR to Localize the Metal-Ion Cofactor in an Oligomeric DnaB Helicase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Strategies for RNA Resonance Assignment byFrontiers in molecular biosciences · 2021Review
- Protein Side-Chain-DNA Contacts Probed by Fast Magic-Angle Spinning NMR.The journal of physical chemistry. B · 2020Article
- Structure of a Protein-RNA Complex by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2020Article
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3 authors.
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Abstract
Solid-state NMR (ssNMR) is applicable to high molecular-weight (MW) protein assemblies in a non-amorphous precipitate. The technique yields atomic resolution structural information on both soluble and insoluble particles without limitations of MW or requirement of crystals. Herein, we propose and demonstrate an approach that yields the structure of protein-RNA complexes (RNP) solely from ssNMR data. Instead of using low-sensitivity magnetization transfer steps between heteronuclei of the protein and the RNA, we measure paramagnetic relaxation enhancement effects elicited on the RNA by a paramagnetic tag coupled to the protein. We demonstrate that this data, together with chemical-shift-perturbation data, yields an accurate structure of an RNP complex, starting from the bound structures of its components. The possibility of characterizing protein-RNA interactions by ssNMR may enable applications to large RNP complexes, whose structures are not accessible by other methods.
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