ArticleJournal of biomolecular NMR2000
Refinement of the protein backbone angle psi in NMR structure calculations.
Article in Journal of biomolecular NMR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 27 citations in OpenAlex.
- NMR evidence for residue-based LFER relationship in two-state folding-unfolding equilibrium of the spectrin SH3 domain in acidic solutions.Biophysics and physicobiology · 2026Article
- 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
- An assignment of intrinsically disordered regions of proteins based on NMR structures.Journal of structural biology · 2013Article
- 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
- Correlated dynamics between protein HN and HC bonds observed by NMR cross relaxation.Journal of the American Chemical Society · 2009Article
- Pairwise NMR experiments for the determination of protein backbone dihedral angle Phi based on cross-correlated spin relaxation.Journal of biomolecular NMR · 2007Article
- A use of Ramachandran potentials in protein solution structure determinations.Journal of biomolecular NMR · 2003Article
- The precision of NMR structure ensembles revisited.Journal of biomolecular NMR · 2003Article
- 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.Journal of biomolecular NMR · 2002Article
- Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.Journal of biomolecular NMR · 2002Article
- Intraresidue 1H-15N-13C' and 1H alpha-13C alpha-13C' dipole-CSA relaxation interference as a source of constraints for structural refinement of metal-binding sites in zinc-finger proteins.Journal of biomolecular NMR · 2001Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Cross-correlated relaxation rates involving the Calpha-Halpha dipolar interaction and the carbonyl (C') chemical shift anisotropy (CSA) have been measured using two complementary 3D experiments. We show that the protein backbone angle psi can be directly refined against such cross-correlated relaxation rates (gammaHalphaCalpha,C') and the three-bond H/D isotope effect on the Calpha chemical shifts (3 deltaCalpha(ND)). By simultaneously using both experimental parameters as restraints during NMR structure calculations, a unique value for the backbone angle psi is defined. We have applied the new refinement method to the alpha-Spectrin SH3 domain (a beta-sheet protein) and to the Sgs1p HRDC domain (an alpha-helical protein) and show that the quality of the NMR structures is substantially improved, judging from the atomic coordinate precision and the Ramachandran map. In addition, the psi-refined NMR structures of the SH3 domain deviate less from the 1.8 A crystal structure, suggesting an improved accuracy. The proposed refinement method can be used to significantly improve the quality of NMR structures and will be applicable to larger proteins.
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