ArticleJournal of biomolecular NMR2002
Exact solutions for chemical bond orientations from residual dipolar couplings.
Article in Journal of biomolecular NMR, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A graphical method for analyzing distance restraints using residual dipolar couplings for structure determination of symmetric protein homo-oligomers.Protein science : a publication of the Protein Society · 2011Article
- Structure-oriented methods for protein NMR data analysis.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- 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
- KinImmerse: Macromolecular VR for NMR ensembles.Source code for biology and medicine · 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
- HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections.Journal of biomolecular NMR · 2007Article
- Exact solutions for internuclear vectors and backbone dihedral angles from NH residual dipolar couplings in two media, and their application in a systematic search algorithm for determining protein backbone structure.Journal of biomolecular NMR · 2004Article
- An expectation/maximization nuclear vector replacement algorithm for automated NMR resonance assignments.Journal of biomolecular NMR · 2004Article
- Protein structure prediction using sparse dipolar coupling data.Nucleic acids research · 2004Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
New methods for determining chemical structures from residual dipolar couplings are presented. The fundamental dipolar coupling equation is converted to an elliptical equation in the principal alignment frame. This elliptical equation is then combined with other angular or dipolar coupling constraints to form simple polynomial equations that define discrete solutions for the unit vector(s). The methods are illustrated with residual dipolar coupling data on ubiquitin taken in a single anisotropic medium. The protein backbone is divided into its rigid groups (namely, its peptide planes and Calpha frames), which may be solved for independently. A simple procedure for recombining these independent solutions results in backbone dihedral angles phi and psi that resemble those of the known native structure. Subsequent refinement of these phi-psi angles by the ROSETTA program produces a structure of ubiquitin that agrees with the known native structure to 1.1 A Calpha rmsd.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.