ArticleProceedings of the National Academy of Sciences of the United States of America2008
Paramagnetic shifts in solid-state NMR of proteins to elicit structural information.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 94 citations in OpenAlex.
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Review
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- Paramagnetic Solid-State NMR to Localize the Metal-Ion Cofactor in an Oligomeric DnaB Helicase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Revisiting paramagnetic relaxation enhancements in slowly rotating systems: how long is the long range?Magnetic resonance (Gottingen, Germany) · 2021Article
- Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine.iScience · 2020Review
- A Double-Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe.Angewandte Chemie (International ed. in English) · 2019Review
- Quantifying Microsecond Exchange in Large Protein Complexes with Accelerated Relaxation Dispersion Experiments in the Solid State.Scientific reports · 2019Article
- Characterization of Protein-Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements.Journal of the American Chemical Society · 2017Article
- New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.Archives of biochemistry and biophysics · 2017Review
- A protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Journal of biomolecular NMR · 2016Article
- Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.Journal of biomolecular NMR · 2016Article
- Information content of long-range NMR data for the characterization of conformational heterogeneity.Journal of biomolecular NMR · 2015Article
- Structural studies of proteins by paramagnetic solid-state NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Solid-state NMR and membrane proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Solid state NMR chemical shift assignment and conformational analysis of a cellulose binding protein facilitated by optimized glycerol enrichment.Journal of biomolecular NMR · 2014Article
- Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Sensitivity and resolution enhanced solid-state NMR for paramagnetic systems and biomolecules under very fast magic angle spinning.Accounts of chemical research · 2013Article
- Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel.Journal of the American Chemical Society · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recent observation of pseudocontact shifts (pcs) in (13)C high-resolution solid-state NMR of paramagnetic proteins opens the way to their application as structural restraints. Here, by investigating a microcrystalline sample of cobalt(II)-substituted matrix metalloproteinase 12 [CoMMP-12 (159 AA, 17.5 kDa)], it is shown that a combined strategy of protein labeling and dilution of the paramagnetic species (i.e., (13)C-,(15)N-labeled CoMMP-12 diluted in unlabeled ZnMMP-12, and (13)C-,(15)N-labeled ZnMMP-12 diluted in unlabeled CoMMP-12) allows one to easily separate the pcs contributions originated from the protein internal metal (intramolecular pcs) from those due to the metals in neighboring proteins in the crystal lattice (intermolecular pcs) and that both can be used for structural purposes. It is demonstrated that intramolecular pcs are significant structural restraints helpful in increasing both precision and accuracy of the structure, which is a need in solid-state structural biology nowadays. Furthermore, intermolecular pcs provide unique information on positions and orientations of neighboring protein molecules in the solid phase.
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