ArticleJournal of biomolecular NMR2011
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR.Nature communications · 2023Article
- Micellar TIA1 with folded RNA binding domains as a model for reversible stress granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Prion Amyloid Polymorphs - The Tag Might Change It All.Frontiers in molecular biosciences · 2020Article
- Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- On the problem of resonance assignments in solid state NMR of uniformly ¹⁵N,¹³C-labeled 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
- Automated robust and accurate assignment of protein resonances for solid state NMR.Journal of biomolecular NMR · 2014Article
- BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.Journal of biomolecular NMR · 2014Article
- SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.Journal of biomolecular NMR · 2013Article
- Automated solid-state NMR resonance assignment of protein microcrystals and amyloids.Journal of biomolecular NMR · 2013Article
- Structural characterization of supramolecular assemblies by ¹³C spin dilution and 3D solid-state NMR.Journal of biomolecular NMR · 2013Article
- Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra.Journal of biomolecular NMR · 2012Article
- Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.Journal of biomolecular NMR · 2012Article
- Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.The journal of physical chemistry. B · 2012Article
- Properties of the DREAM scheme and its optimization for application to proteins.Journal of biomolecular NMR · 2012Article
- Simultaneous acquisition of PAR and PAIN spectra.Journal of biomolecular NMR · 2012Article
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9 authors.
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Abstract
We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled protein sample, sequential chemical-shift information for 74% of the N, Cα, Cβ triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the assignment of this largest protein assigned today by solid-state NMR, and for which no solution-state NMR shifts were available. A comparison of the NMR chemical shifts with crystallographic data reveals that regions with high crystallographic B-factors are particularly difficult to assign. While the secondary structure elements derived from the chemical shift data correspond mainly to those present in the X-ray crystal structure, we detect an additional helical element and structural variability in the protein crystal, most probably originating from the different molecules in the asymmetric unit, with the observation of doubled resonances in several parts, including entire stretches, of the protein. Our results provide the point of departure towards an atomic-resolution structural analysis of the C-terminal Ure2p domain in the context of the full-length prion fibrils.
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