ArticleJournal of the American Chemical Society2009
One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Probing Protein-Protein Interactions Using Asymmetric Labeling and Carbonyl-Carbon Selective Heteronuclear NMR Spectroscopy.Molecules (Basel, Switzerland) · 2018Review
- Simultaneous detection of intra- and inter-molecular paramagnetic relaxation enhancements in protein complexes.Journal of biomolecular NMR · 2018Article
- Time-shared experiments for efficient assignment of triple-selectively labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- A mechanism for the auto-inhibition of hyperpolarization-activated cyclic nucleotide-gated (HCN) channel opening and its relief by cAMP.The Journal of biological chemistry · 2014Article
- Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment.Journal of biomolecular NMR · 2012Article
- Characterizing weak protein-protein complexes by NMR residual dipolar couplings.European biophysics journal : EBJ · 2011Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We present a procedure that supports the acquisition of (1)H-(15)N residual dipolar coupling (RDC) values for individual subunits in binary or ternary protein assemblies from a single experimental sample. Our method relies on asymmetric labeling of each subunit with the following scheme: species A uniformly with (15)N, species B uniformly with (15)N and (13)C, and species C uniformly with (15)N but selectively with (13)C' or (13)C(alpha). Because only a single sample is required, the approach obviates the need for preparing multiple samples and eliminates potential errors introduced from differences in sample conditions. Because numerous biological processes rely on protein assemblies or transient interactions, this method should be well suited for a wide range of future applications.
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