ArticleJournal of the American Chemical Society2009
Accurate sampling of high-frequency motions in proteins by steady-state (15)N-{(1)H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation.
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 40 papers.
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40 citing papers in PubMed.
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- Role of Backbone Dynamics in Modulating the Interactions of Disordered Ligands with the TAZ1 Domain of the CREB-Binding Protein.Biochemistry · 2019Article
- In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins.Proteomics · 2019Review
- An NMR strategy to detect conformational differences in a protein complexed with highly analogous inhibitors in solution.Methods (San Diego, Calif.) · 2018Article
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- Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase fromThe Journal of biological chemistry · 2017Article
- Solution structure of domain 1.1 of the σThe Journal of biological chemistry · 2017Article
- Characterization of DNA Binding by the Isolated N-Terminal Domain of Vaccinia Virus DNA Topoisomerase IB.Biochemistry · 2017Article
- Article
- Structure of the C-Terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase.Biochemistry · 2016Article
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3 authors.
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Abstract
The steady-state {(1)H}-(15)N NOE experiment is used in most common NMR analyses of backbone dynamics to accurately ascertain the effects of the fast dynamic modes. We demonstrate here that, in its most common implementation, this experiment generates an incorrect steady state in the presence of CSA/dipole cross-correlated relaxation leading to large errors in the characterization of these high-frequency modes. This affects both the quantitative and qualitative interpretation of (15)N backbone relaxation in dynamic terms. We demonstrate further that minor changes in the experimental implementation effectively remove these errors and allow a more accurate interpretation of protein backbone dynamics.
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