ArticleJournal of biomolecular NMR2000
Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings.
Article in Journal of biomolecular NMR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 38 citations in OpenAlex.
- Measurement of (1)H-(15)N and (1)H-(13)C residual dipolar couplings in nucleic acids from TROSY intensities.Journal of biomolecular NMR · 2011Article
- High-resolution protein structure determination starting with a global fold calculated from exact solutions to the RDC equations.Journal of biomolecular NMR · 2009Article
- Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- 16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination.Journal of the American Chemical Society · 2008Article
- Top-down approach in protein RDC data analysis: de novo estimation of the alignment tensor.Journal of biomolecular NMR · 2007Article
- Statistical coil model of the unfolded state: resolving the reconciliation problem.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Backbone assignment of proteins with known structure using residual dipolar couplings.Journal of biomolecular NMR · 2004Article
- Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids.Journal of biomolecular NMR · 2004Article
- Improvement of hydrogen bond geometry in protein NMR structures by residual dipolar couplings--an assessment of the interrelation of NMR restraints.Journal of biomolecular NMR · 2004Article
- Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data.Biophysical journal · 2002Article
- Exact solutions for chemical bond orientations from residual dipolar couplings.Journal of biomolecular NMR · 2002Article
- Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein.Journal of biomolecular NMR · 2001Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Residual dipolar couplings measured in weakly aligning liquid-crystalline solvent contain valuable information on the structure of biomolecules in solution. Here we demonstrate that dipolar couplings (DCs) can be used to derive a comprehensive set of pairwise angular restraints that do not depend on the orientation of the alignment tensor principal axes. These restraints can be used to assess the agreement between a trial protein structure and a set of experimental dipolar couplings by means of a graphic representation termed a 'DC consistency map'. Importantly, these maps can be used to recognize structural elements consistent with the experimental DC data and to identify structural parameters that require further refinement, which could prove important for the success of DC-based structure calculations. This approach is illustrated for the 42 kDa maltodextrin-binding protein.
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