ArticleNucleic acids research2004
Protein structure prediction using sparse dipolar coupling data.
Article in Nucleic acids research, 2004. 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.
- Residue proximity information and protein model discrimination using saturation-suppressor mutagenesis.eLife · 2015Article
- One contact for every twelve residues allows robust and accurate topology-level protein structure modeling.Proteins · 2014Article
- Modeling helical proteins using residual dipolar couplings, sparse long-range distance constraints and a simple residue-based force field.Theoretical chemistry accounts · 2013Article
- HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections.Journal of biomolecular NMR · 2007Article
- Exploring conformational space using a mean field technique with MOLS sampling.Journal of biosciences · 2007Review
- Spin-labeled analogs of CMP-NeuAc as NMR probes of the alpha-2,6-sialyltransferase ST6Gal I.Chemistry & biology · 2007Article
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Authors and funding
4 authors.
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Abstract
Residual dipolar coupling (RDC) represents one of the most exciting emerging NMR techniques for protein structure studies. However, solving a protein structure using RDC data alone is still a highly challenging problem. We report here a computer program, RDC-PROSPECT, for protein structure prediction based on a structural homolog or analog of the target protein in the Protein Data Bank (PDB), which best aligns with the (15)N-(1)H RDC data of the protein recorded in a single ordering medium. Since RDC-PROSPECT uses only RDC data and predicted secondary structure information, its performance is virtually independent of sequence similarity between a target protein and its structural homolog/analog, making it applicable to protein targets beyond the scope of current protein threading techniques. We have tested RDC-PROSPECT on all (15)N-(1)H RDC data (representing 43 proteins) deposited in the BioMagResBank (BMRB) database. The program correctly identified structural folds for 83.7% of the target proteins, and achieved an average alignment accuracy of 98.1% residues within a four-residue shift.
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