ArticleJournal of biomolecular NMR2011
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 40 citations in OpenAlex.
- Quantitative Agreement between Conformational Substates of Holo Calcium-Loaded Calmodulin Detected by Double Electron-Electron Resonance EPR and Predicted by Molecular Dynamics Simulations.Journal of the American Chemical Society · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- The Photocatalyzed Thiol-ene reaction: A New Tag to Yield Fast, Selective and reversible Paramagnetic Tagging of Proteins.Chemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Covalency and magnetic anisotropy in lanthanide single molecule magnets: the DyDOTA archetype.Chemical science · 2019Article
- Identification of productive and futile encounters in an electron transfer protein complex.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags.Journal of biomolecular NMR · 2016Article
- Information content of long-range NMR data for the characterization of conformational heterogeneity.Journal of biomolecular NMR · 2015Article
- Compact, hydrophilic, lanthanide-binding tags for paramagnetic NMR spectroscopy.Chemical science · 2015Article
- A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy.Journal of biomolecular NMR · 2015Article
- Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015Article
- FANTEN: a new web-based interface for the analysis of magnetic anisotropy-induced NMR data.Journal of biomolecular NMR · 2015Article
- Insights into domain-domain motions in proteins and RNA from solution NMR.Accounts of chemical research · 2014Review
- 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
- Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state.The Journal of biological chemistry · 2013Article
- MaxOcc: a web portal for maximum occurrence analysis.Journal of biomolecular NMR · 2012Article
- Transient, sparsely populated compact states of apo and calcium-loaded calmodulin probed by paramagnetic relaxation enhancement: interplay of conformational selection and induced fit.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramagnetism-based restraints. These restraints were measured after inclusion of a lanthanide binding tag in the C-terminal domain to supplement the data obtained by substitution of three paramagnetic lanthanide ions to the calcium ion in the second calcium binding loop of the N-terminal domain. The analysis shows that the availability of paramagnetic restraints arising from metal ions placed on both domains, reduces the MO of the conformations to different extents, thereby helping to identify those conformations that can be mostly sampled by the protein.
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Registered trials
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.