ArticleJournal of the American Chemical Society2008
16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Solution Domain Dynamics of Monomeric SARS-CoV‑2 Main Protease Revealed by Optimized NMR Residual Dipolar Coupling Measurements.ACS physical chemistry Au · 2026Article
- Use of Measured Residual Dipolar Couplings to Calculate Residual Dipolar Couplings for a Protein Structure: A Case Study Using Hen Egg-White Lysozyme.Journal of chemical information and modeling · 2025Article
- Integrated NMR/Molecular Dynamics Determination of the Ensemble Conformation of a Thermodynamically Stable CUUG RNA Tetraloop.Journal of the American Chemical Society · 2023Article
- Partial alignment, residual dipolar couplings and molecular symmetry in solution NMR.Journal of biomolecular NMR · 2019Article
- Re-evaluating the p7 viroporin structure.Nature · 2018Article
- Correlated inter-domain motions in adenylate kinase.PLoS computational biology · 2014Article
- Equivalence between Euler angle conventions for the description of tensorial interactions in liquid NMR: application to different software programs.Journal of biomolecular NMR · 2013Review
- Modeling helical proteins using residual dipolar couplings, sparse long-range distance constraints and a simple residue-based force field.Theoretical chemistry accounts · 2013Article
- Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles.Journal of biomolecular NMR · 2013Article
- Characterizing weak protein-protein complexes by NMR residual dipolar couplings.European biophysics journal : EBJ · 2011Review
- Ca2+ binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the Na+/Ca2+ exchanger.The Journal of biological chemistry · 2011Article
- Topology and immersion depth of an integral membrane protein by paramagnetic rates from dissolved oxygen.Journal of biomolecular NMR · 2011Article
- Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Journal of the American Chemical Society · 2011Article
- Toward a unified representation of protein structural dynamics in solution.Journal of the American Chemical Society · 2009Article
- High-resolution protein structure determination starting with a global fold calculated from exact solutions to the RDC equations.Journal of biomolecular NMR · 2009Article
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Authors and funding
6 authors.
Funding
Abstract
Residual dipolar couplings (RDCs) measured for internally rigid molecular fragments provide important information about the relative orientations of these fragments. Dependent on the symmetry of the alignment tensor and the symmetry of the molecular fragment, however, there generally exist more than one solution for the fragment orientation consistent with the measured RDCs. Analytical solutions are presented that describe the complete set of orientations of internally rigid fragments that are consistent with multiple dipolar couplings measured in a single alignment medium that is rhombic. For the first time, it is shown that, for a planar fragment such as the peptide plane, there generally exist 16 different solutions with their analytical expressions presented explicitly. The presence of these solutions is shown to be highly relevant for standard structure determination protocols using RDCs to refine molecular structures. In particular, when using standard protein structure refinement with RDCs that were measured in a single alignment medium as constraints, it is found that often more than one of the peptide plane solutions is physically viable; i.e., despite being consistent with measured RDCs, the local backbone structure can be incorrect. On the basis of experimental and simulated examples, it is rationalized why protein structures that are refined against RDCs measured in a single medium can have lower resolution (precision) than one would expect on the basis of the experimental accuracy of the RDCs. Conditions are discussed under which the correct solution can be identified.
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