ArticleJournal of biomolecular NMR2012
Improved chemical shift prediction by Rosetta conformational sampling.
Article in Journal of biomolecular NMR, 2012. 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, 6 citations in OpenAlex.
- Structural basis for therapeutic inhibition of complement C5.Nature structural & molecular biology · 2016Article
- acACS: improving the prediction accuracy of protein subcellular locations and protein classification by incorporating the average chemical shifts composition.TheScientificWorldJournal · 2014Article
- Solid state NMR and protein-protein interactions in membranes.Current opinion in structural biology · 2013Review
- Membrane protein structure determination in membrana.Accounts of chemical research · 2013Article
- Chemical shifts in biomolecules.Current opinion in structural biology · 2013Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Chemical shift frequencies represent a time-average of all the conformational states populated by a protein. Thus, chemical shift prediction programs based on sequence and database analysis yield higher accuracy for rigid rather than flexible protein segments. Here we show that the prediction accuracy can be significantly improved by averaging over an ensemble of structures, predicted solely from amino acid sequence with the Rosetta program. This approach to chemical shift and structure prediction has the potential to be useful for guiding resonance assignments, especially in solid-state NMR structural studies of membrane proteins in proteoliposomes.
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Registered trials
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