ArticleJournal of biomolecular NMR2002
Breaking symmetry in the structure determination of (large) symmetric protein dimers.
Article in Journal of biomolecular NMR, 2002. 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.
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- NMR pseudocontact shifts in a symmetric protein homotrimer.Journal of biomolecular NMR · 2020Article
- A Double-Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe.Angewandte Chemie (International ed. in English) · 2019Review
- Localization of ligands within human carbonic anhydrase II usingChemical science · 2019Article
- Conformationally locked lanthanide chelating tags for convenient pseudocontact shift protein nuclear magnetic resonance spectroscopy.Journal of biomolecular NMR · 2018Article
- Paramagnetic Ligand Tagging To Identify Protein Binding Sites.Journal of the American Chemical Society · 2015Article
- Multiple paramagnetic effects through a tagged reporter protein.Angewandte Chemie (International ed. in English) · 2015Article
- Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.Molecules (Basel, Switzerland) · 2013Review
- How reliable are pseudocontact shifts induced in proteins and ligands by mobile paramagnetic metal tags? A modelling study.Journal of biomolecular NMR · 2013Article
- Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.Journal of biomolecular NMR · 2012Article
- Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects.Progress in nuclear magnetic resonance spectroscopy · 2011Review
- Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR.Journal of biomolecular NMR · 2011Article
- Engineering encodable lanthanide-binding tags into loop regions of proteins.Journal of the American Chemical Society · 2011Article
- Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density.Journal of biomolecular NMR · 2010Article
- PCS-based structure determination of protein-protein complexes.Journal of biomolecular NMR · 2010Article
- An NMR structural study of nickel-substituted rubredoxin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- Paramagnetic labelling of proteins and oligonucleotides for NMR.Journal of biomolecular NMR · 2010Review
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect.Journal of biomolecular NMR · 2009Article
- High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment.Journal of biomolecular NMR · 2008Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We demonstrate a novel methodology to disrupt the symmetry in the NMR spectra of homodimers. A paramagnetic probe is introduced sub-stoichiometrically to create an asymmetric system with the paramagnetic probe residing on only one monomer within the dimer. This creates sufficient magnetic anisotropy for resolution of symmetry-related overlapped resonances and, consequently, detection of pseudocontact shifts and residual dipolar couplings specific to each monomeric component. These pseudocontact shifts can be readily incorporated into existing structure refinement calculations and enable determination of monomer orientation within the dimeric protein. This methodology can be widely used for solution structure determination of symmetric dimers.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.