ArticleJournal of biomolecular NMR2003
Measurement of residual dipolar couplings from 1Halpha to 13Calpha and 15N using a simple HNCA-based experiment.
Article in Journal of biomolecular NMR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Solution structure, dynamics and tetrahedral assembly of Anti-TRAP, a homo-trimeric triskelion-shaped regulator of tryptophan biosynthesis inJournal of structural biology: X · 2024Article
- Hybrid Approaches to Structural Characterization of Conformational Ensembles of Complex Macromolecular Systems Combining NMR Residual Dipolar Couplings and Solution X-ray Scattering.Chemical reviews · 2016Review
- Real-time pure shift ¹⁵N HSQC of proteins: a real improvement in resolution and sensitivity.Journal of biomolecular NMR · 2015Article
- CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.BMC structural biology · 2010Article
- MQ-HNCO-TROSY for the measurement of scalar and residual dipolar couplings in larger proteins: application to a 557-residue IgFLNa16-21.Journal of biomolecular NMR · 2010Article
- Hydrophobic core mutations in CI2 globally perturb fast side-chain dynamics similarly without regard to position.Biochemistry · 2008Article
- A set of HA-detected experiments for measuring scalar and residual dipolar couplings.Journal of biomolecular NMR · 2005Article
- Efficient and precise measurement of H(alpha)-C(alpha), C(alpha)-C', C(alpha)-C(beta) and H(N)-N residual dipolar couplings from 2D H(N)-N correlation spectra.Journal of biomolecular NMR · 2005Article
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1 author.
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Abstract
Novel NMR pulse schemes for simultaneous measurement of 1D(C)alpha(H)alpha and 2D(NH)alpha residual dipolar couplings in proteins is presented. We show that 2D(NH)alpha coupling can be very useful for protein structure determination. The 2D(NH)alpha coupling can be measured from 15N dimension with good accuracy on a slowly relaxing TROSY resonance, utilizing HNCA-TROSY-based experiments, which concomitantly supply large 1D(C)alpha(H)alpha coupling. The dynamic range of 2D(NH)alpha coupling is comparable to 1D(NC') coupling, but instead, it also serves non-redundant information on the course of protein backbone, thanks to rotational degree of freedom with respect to peptide bond. The HNCA-TROSY-based experiments are optimal for measuring residual dipolar couplings at high magnetic fields owing to absence of rapid transverse relaxation of carbonyl carbon. The reliability of the proposed approach was tested on 15N/13C human ubiquitin. A very good correlation with ubiquitin solution as well as crystal structure, for both 1D(C)alpha(H)alpha and 2D(NH)alpha couplings, was obtained.
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