ArticleProtein science : a publication of the Protein Society2015
Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Rapid Quantification of Protein Secondary Structure Composition from a Single Unassigned 1DJournal of the American Chemical Society · 2024Article
- Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR.Nature communications · 2023Article
- Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD.Journal of structural biology: X · 2023Article
- Maturation of the functional mouse CRES amyloid from globular form.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- High resolution observed in 800 MHz DNP spectra of extremely rigid type III secretion needles.Journal of biomolecular NMR · 2016Article
- Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Observing the overall rocking motion of a protein in a crystal.Nature communications · 2015Article
- Molecular Dynamics Simulations of Macromolecular Crystals.Wiley interdisciplinary reviews. Computational molecular scienceArticle
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By applying [1-(13) C]- and [2-(13) C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and the collection of a wealth of long-range distance information. A high precision solid-state NMR structure of microcrystalline ubiquitin was calculated with a backbone rmsd of 1.57 to the X-ray structure and 1.32 Å to the solution NMR structure. Interestingly, we can resolve structural heterogeneity as the presence of three slightly different conformations. Structural heterogeneity is most significant for the loop region β1-β2 but also for β-strands β1, β2, β3, and β5 as well as for the loop connecting α1 and β3. This structural polymorphism observed in the solid-state NMR spectra coincides with regions that showed dynamics in solution NMR experiments on different timescales.
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