ArticleProceedings of the National Academy of Sciences of the United States of America2008
Dipole tensor-based atomic-resolution structure determination of a nanocrystalline protein by solid-state NMR.
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 69 papers.
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69 citing papers in PubMed.
- In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.The journal of physical chemistry. B · 2026Article
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- Analysis of the MODIST Sequence for Selective Proton-Proton Recoupling.The journal of physical chemistry. A · 2025Article
- 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
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- Atomic-Resolution Structure of the Protein Encoded by Gene V of fd Bacteriophage in Complex with Viral ssDNA Determined by Magic-Angle Spinning Solid-State NMR.Journal of the American Chemical Society · 2023Article
- A Cholesterol Dimer Stabilizes the Inactivated State of an Inward-Rectifier Potassium Channel.Angewandte Chemie (International ed. in English) · 2022Article
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Rapid automated determination of chemical shift anisotropy values in the carbonyl and carboxyl groups of fd-y21m bacteriophage using solid state NMR.Journal of biomolecular NMR · 2018Article
- New applications of solid-state NMR in structural biology.Emerging topics in life sciences · 2018Article
- Solid-State NMR of highlyMethods (San Diego, Calif.) · 2018Article
- Fast Magic-Angle-SpinningThe journal of physical chemistry. B · 2018Article
- Xplor-NIH for molecular structure determination from NMR and other data sources.Protein science : a publication of the Protein Society · 2018Article
- Ubiquitin immobilized on mesoporous MCM41 silica surfaces - Analysis by solid-state NMR with biophysical and surface characterization.Biointerphases · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.Nature structural & molecular biology · 2016Article
- Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015Review
- Review
9 more citing papers are in PubMed but not listed here.
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Abstract
Magic-angle spinning (MAS) solid-state NMR (SSNMR) techniques have emerged in recent years for solving complete structures of uniformly labeled proteins lacking macroscopic order. Strategies used thus far have relied primarily on semiquantitative distance restraints, analogous to the nuclear Overhauser effect (NOE) routinely used in solution NMR. Here, we present a complementary approach for using relative orientations of molecular fragments, determined from dipolar line shapes. Whereas SSNMR distance restraints typically have an uncertainty of approximately 1 A, the tensor-based experiments report on relative vector (pseudobond) angles with precision of a few degrees. By using 3D techniques of this type, vector angle (VEAN) restraints were determined for the majority of the 56-residue B1 immunoglobulin binding domain of protein G [protein GB1 (a total of 47 HN-HN, 49 HN-HC, and 12 HA-HB restraints)]. By using distance restraints alone in the structure calculations, the overall backbone root-mean-square deviation (bbRMSD) was 1.01 +/- 0.13 A (1.52 +/- 0.12 A for all heavy atoms), which improved to 0.49 +/- 0.05 A (1.19 +/- 0.07 A) on the addition of empirical chemical shift [torsion angle likelihood obtained from shift and sequence similarity (TALOS)] restraints. VEAN restraints further improved the ensemble to 0.31 +/- 0.06 A bbRMSD (1.06 +/- 0.07 A); relative to the structure with distances alone, most of the improvement remained (bbRMSD 0.64 +/- 0.09 A; 1.29 +/- 0.07 A) when TALOS restraints were removed before refinement. These results represent significant progress toward atomic-resolution protein structure determination by SSNMR, capabilities that can be applied to a large range of membrane proteins and fibrils, which are often not amenable to solution NMR or x-ray crystallography.
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