ArticleJournal of biomolecular NMR2007
Pairwise NMR experiments for the determination of protein backbone dihedral angle Phi based on cross-correlated spin relaxation.
Article in Journal of biomolecular NMR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 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
- Direct Investigation of Slow Correlated Dynamics in Proteins via Dipolar Interactions.Journal of the American Chemical Society · 2016Article
- 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
- Precise structural determination of weakly binding peptides by utilizing dihedral angle constraints.Journal of biomolecular NMR · 2010Article
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Novel cross-correlated spin relaxation (CCR) experiments are described, which measure pairwise CCR rates for obtaining peptide dihedral angles Phi. The experiments utilize intra-HNCA type coherence transfer to refocus 2-bond JNCalpha coupling evolution and generate the N(i)-Calpha(i) or C'(i-1)-Calpha(i) multiple quantum coherences which are required for measuring the desired CCR rates. The contribution from other coherences is also discussed and an appropriate setting of the evolution delays is presented. These CCR experiments were applied to 15N- and 13C-labeled human ubiquitin. The relevant CCR rates showed a high degree of correlation with the Phi angles observed in the X-ray structure. By utilizing these CCR experiments in combination with those previously established for obtaining dihedral angle Psi, we can determine high resolution structures of peptides that bind weakly to large target molecules.
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