ArticleProceedings of the National Academy of Sciences of the United States of America2011
Ultrahigh resolution protein structures using NMR chemical shift tensors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed.
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- Rapid Quantification of Protein Secondary Structure Composition from a Single Unassigned 1DJournal of the American Chemical Society · 2024Article
- Solid-State NMRJournal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Cross polarization stability in multidimensional NMR spectroscopy of biological solids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024Article
- Fungicidal amphotericin B sponges are assemblies of staggered asymmetric homodimers encasing large void volumes.Nature structural & molecular biology · 2021Article
- Off-resonanceJournal of biomolecular NMR · 2021Article
- Dipolar Order Parameters in Large Systems With Fast Spinning.Frontiers in molecular biosciences · 2021Article
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Scaled recoupling of chemical shift anisotropies at high magnetic fields under MAS with interspersed C-elements.The Journal of chemical physics · 2020Article
- Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-RangeThe journal of physical chemistry. B · 2020Article
- Maturation of the functional mouse CRES amyloid from globular form.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Accurate BackboneChemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Multi-receiver solid-state NMR using polarization optimized experiments (POE) at ultrafast magic angle spinning.Journal of biomolecular NMR · 2020Article
- Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 inBiomolecules · 2020Article
- Inferring protein 3D structure from deep mutation scans.Nature genetics · 2019Article
- High-Sensitivity Detection of NanometerThe journal of physical chemistry. B · 2019Article
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Abstract
NMR chemical shift tensors (CSTs) in proteins, as well as their orientations, represent an important new restraint class for protein structure refinement and determination. Here, we present the first determination of both CST magnitudes and orientations for (13)Cα and (15)N (peptide backbone) groups in a protein, the β1 IgG binding domain of protein G from Streptococcus spp., GB1. Site-specific (13)Cα and (15)N CSTs were measured using synchronously evolved recoupling experiments in which (13)C and (15)N tensors were projected onto the (1)H-(13)C and (1)H-(15)N vectors, respectively, and onto the (15)N-(13)C vector in the case of (13)Cα. The orientations of the (13)Cα CSTs to the (1)H-(13)C and (13)C-(15)N vectors agreed well with the results of ab initio calculations, with an rmsd of approximately 8°. In addition, the measured (15)N tensors exhibited larger reduced anisotropies in α-helical versus β-sheet regions, with very limited variation (18 ± 4°) in the orientation of the z-axis of the (15)N CST with respect to the (1)H-(15)N vector. Incorporation of the (13)Cα CST restraints into structure calculations, in combination with isotropic chemical shifts, transferred echo double resonance (13)C-(15)N distances and vector angle restraints, improved the backbone rmsd to 0.16 Å (PDB ID code 2LGI) and is consistent with existing X-ray structures (0.51 Å agreement with PDB ID code 2QMT). These results demonstrate that chemical shift tensors have considerable utility in protein structure refinement, with the best structures comparable to 1.0-Å crystal structures, based upon empirical metrics such as Ramachandran geometries and χ(1)/χ(2) distributions, providing solid-state NMR with a powerful tool for de novo structure determination.
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