ArticleJournal of biomolecular NMR2002
TROSY experiment for refinement of backbone psi and phi by simultaneous measurements of cross-correlated relaxation rates and 3,4J(H alpha HN) coupling constants.
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 6 papers.
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Who cites it
6 citing papers in PubMed.
- Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Review
- Cross-correlated relaxation rates between protein backbone H-X dipolar interactions.Journal of biomolecular NMR · 2017Article
- How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar Cα-C'/H N-N cross-correlated relaxation.Journal of biomolecular NMR · 2011Article
- Side chain: backbone projections in aromatic and ASX residues from NMR cross-correlated relaxation.Journal of biomolecular NMR · 2010Article
- Correlated dynamics between protein HN and HC bonds observed by NMR cross relaxation.Journal of the American Chemical Society · 2009Article
- Measurement of residual dipolar couplings from 1Halpha to 13Calpha and 15N using a simple HNCA-based experiment.Journal of biomolecular NMR · 2003Article
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2 authors.
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Abstract
The TROSY principle has been introduced into a HNCA experiment, which is designed for measurements of the intraresidual and sequential H(alpha)-C(alpha)/H(N)-N dipole/dipole and H(alpha)-C(alpha)/N dipole/CSA cross-correlated relaxation rates. In addition, the new experiment provides values of the (3,4)J(H alpha HN) coupling constants measured in an E.COSY manner. The conformational restraints for the psi and phi angles are obtained through the use of the cross-correlated relaxation rates together with the Karplus-type dependencies of the coupling constants. Improved signal-to-noise is achieved through preservation of all coherence transfer pathways and application of the TROSY principle. The application of the [(15)N,(13)C]-DQ/ZQ-[(15)N,(1)H]-TROSY-E.COSY experiment to the 16 kDa apo-form of the E. coli Heme Chaperon protein CcmE is described. Overall good agreement is achieved between psi and phi angles measured with the new experiment and the average values determined from an ensemble of 20 NMR conformers.
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