ArticleNature chemistry2012
Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy.
Article in Nature chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
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- DNP enhanced solid-state NMR of lattice-like microcrystalline protein assemblies facilitated by co-assembly with dinitroxide-tagged proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Review
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants.Chemical reviews · 2022Review
- Structure of membrane diacylglycerol kinase in lipid bilayers.Communications biology · 2021Article
- Structure of a Protein-RNA Complex by Solid-State NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2020Article
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
- Two decades of progress in structural and dynamic studies of amyloids by solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Review
- Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy.Journal of structural biology · 2019Article
- Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy.Journal of the American Chemical Society · 2018Article
- Electron decoupling with cross polarization and dynamic nuclear polarization below 6 K.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Methods (San Diego, Calif.) · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.Nature communications · 2017Article
- Rapid Quantitative Measurements of Paramagnetic Relaxation Enhancements in Cu(II)-Tagged Proteins by Proton-Detected Solid-State NMR Spectroscopy.The journal of physical chemistry letters · 2017Article
- New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.Archives of biochemistry and biophysics · 2017Review
- GdJournal of biomolecular NMR · 2017Article
- The Target of β-Expansin EXPB1 in Maize Cell Walls from Binding and Solid-State NMR Studies.Plant physiology · 2016Article
- Gd(iii) and Mn(ii) complexes for dynamic nuclear polarization: small molecular chelate polarizing agents and applications with site-directed spin labeling of proteins.Physical chemistry chemical physics : PCCP · 2016Article
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Authors and funding
5 authors.
Funding
Abstract
Biomacromolecules that are challenging for the usual structural techniques can be studied with atomic resolution by solid-state NMR spectroscopy. However, the paucity of distance restraints >5 Å, traditionally derived from measurements of magnetic dipole-dipole couplings between protein nuclei, is a major bottleneck that hampers such structure elucidation efforts. Here, we describe a general approach that enables the rapid determination of global protein fold in the solid phase via measurements of nuclear paramagnetic relaxation enhancements (PREs) in several analogues of the protein of interest containing covalently attached paramagnetic tags, without the use of conventional internuclear distance restraints. The method is demonstrated using six cysteine-EDTA-Cu(2+) mutants of the 56-residue B1 immunoglobulin-binding domain of protein G, for which ~230 longitudinal backbone (15)N PREs corresponding to distances of ~10-20 Å were obtained. The mean protein fold determined in this manner agrees with the X-ray structure with a backbone atom root-mean-square deviation of 1.8 Å.
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