ArticleJournal of biomolecular NMR2001
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.
Article in Journal of biomolecular NMR, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Cross correlation rates between Curie spin and dipole-dipole relaxation in paramagnetic proteins: the case of cerium substituted calbindin D9k.Journal of biomolecular NMR · 2002Article
- Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.Journal of biomolecular NMR · 2002Article
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3 authors.
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Abstract
1H(i)-15 N(i)-13C'(i) dipole-chemical shift anisotropy (CSA) relaxation interference was quantified for the 13C,15N labeled zinc-finger protein qCRP2(LIM2). The cross-correlation rates obtained for residues located in the metal coordination sites of qCRP2(LIM2) show a high degree of correlation with the peptide plane torsion angles phi and psi taken from the solution structure. 1H(i)-15N(i)-13C'(i) as well as 13C alpha(i)-1H alpha(i)-13C'(i) dipole-CSA cross-correlation rates were subsequently used to improve the geometry of the metal binding site. The optimized dihedral angles of the two zinc-binding sites in qCRP2(LIM2) are in better agreement with values obtained from crystal structures of other zinc-finger proteins and thus establish the utility of this approach to improve the metal-binding site geometry of zinc-finger proteins studied by NMR spectroscopy in solution.
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