ArticleJournal of biomolecular NMR2010
A device for the measurement of residual chemical shift anisotropy and residual dipolar coupling in soluble and membrane-associated proteins.
Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Residual Chemical Shift Anisotropies in the Structure Determination of Small Molecules.Magnetic resonance in chemistry : MRC · 2026Review
- Two-conformer equilibrium of maltose-binding protein in the absence of ligand from residual dipolar coupling analysis.Protein science : a publication of the Protein Society · 2026Article
- Relative configuration of micrograms of natural compounds using proton residual chemical shift anisotropy.Nature communications · 2020Article
- Structural basis of UCUU RNA motif recognition by splicing factor RBM20.Nucleic acids research · 2020Article
- Complex macrocycle exploration: parallel, heuristic, and constraint-based conformer generation using ForceGen.Journal of computer-aided molecular design · 2019Article
- Article
- Synthesis and O-Glycosidic Linkage Conformational Analysis ofThe Journal of organic chemistry · 2019Article
- Application of anisotropic NMR parameters to the confirmation of molecular structure.Nature protocols · 2019Article
- Enhanced measurement of residual chemical shift anisotropy for small molecule structure elucidation.Chemical communications (Cambridge, England) · 2018Article
- Mollib: a molecular and NMR data analysis software.Journal of biomolecular NMR · 2017Article
- Conformational Populations of β-(1→4) O-Glycosidic Linkages Using Redundant NMR J-Couplings and Circular Statistics.The journal of physical chemistry. B · 2017Article
- Unequivocal determination of complex molecular structures using anisotropic NMR measurements.Science (New York, N.Y.) · 2017Article
- Nuclear Magnetic Resonance Insight into the Multiple Glycosaminoglycan Binding Modes of the Link Module from Human TSG-6.Biochemistry · 2016Article
- Ensembles of a small number of conformations with relative populations.Journal of biomolecular NMR · 2015Article
- Spatial reorientation experiments for NMR of solids and partially oriented liquids.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- NMR studies of dynamic biomolecular conformational ensembles.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Structural characterization of a flexible two-domain protein in solution using small angle X-ray scattering and NMR data.Structure (London, England : 1993) · 2014Article
- Improvements to REDCRAFT: a software tool for simultaneous characterization of protein backbone structure and dynamics from residual dipolar couplings.Journal of biomolecular NMR · 2014Article
- Advances in the REDCAT software package.BMC bioinformatics · 2013Article
- Chemokine oligomerization in cell signaling and migration.Progress in molecular biology and translational science · 2013Review
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2 authors.
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Abstract
Residual dipolar coupling (RDC) and residual chemical shift anisotropy (RCSA) report on orientational properties of a dipolar bond vector and a chemical shift anisotropy principal axis system, respectively. They can be highly complementary in the analysis of backbone structure and dynamics in proteins as RCSAs generally include a report on vectors out of a peptide plane while RDCs usually report on in-plane vectors. Both RDC and RCSA average to zero in isotropic solutions and require partial orientation in a magnetic field to become observable. While the alignment and measurement of RDC has become routine, that of RCSA is less common. This is partly due to difficulties in providing a suitable isotopic reference spectrum for the measurement of the small chemical shift offsets coming from RCSA. Here we introduce a device (modified NMR tube) specifically designed for accurate measurement of reference and aligned spectra for RCSA measurements, but with a capacity for RDC measurements as well. Applications to both soluble and membrane anchored proteins are illustrated.
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