ArticleJournal of biomolecular NMR2003
Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints.
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 5 papers.
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Who cites it
5 citing papers in PubMed.
- An improved algorithm for MFR fragment assembly.Journal of biomolecular NMR · 2012Article
- Article
- Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media.Journal of biomolecular NMR · 2008Article
- Exact solutions for internuclear vectors and backbone dihedral angles from NH residual dipolar couplings in two media, and their application in a systematic search algorithm for determining protein backbone structure.Journal of biomolecular NMR · 2004Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the determination of the global fold of human ubiquitin using protein backbone NMR residual dipolar coupling and long-range nuclear Overhauser effect (NOE) data as conformational restraints. Specifically, by use of a maximum of three backbone residual dipolar couplings per residue (Ni-H N i, Ni-C'(i-1), H N i - C'(i-1)) in two tensor frames and only backbone H N -H N NOEs, a global fold of ubiquitin can be derived with a backbone root-mean-square deviation of 1.4 A with respect to the crystal structure. This degree of accuracy is more than adequate for use in databases of structural motifs, and suggests a general approach for the determination of protein global folds using conformational restraints derived only from backbone atoms.
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Registered trials
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