ArticleStructure (London, England : 1993)2013
Modeling proteins using a super-secondary structure library and NMR chemical shift information.
Article in Structure (London, England : 1993), 2013. 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.
- On the use of direct-coupling analysis with a reduced alphabet of amino acids combined with super-secondary structure motifs for protein fold prediction.NAR genomics and bioinformatics · 2021Article
- Protein structural motifs in prediction and design.Current opinion in structural biology · 2017Review
- Development of a motif-based topology-independent structure comparison method to identify evolutionarily related folds.Proteins · 2016Article
- Tertiary alphabet for the observable protein structural universe.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Modularity of Protein Folds as a Tool for Template-Free Modeling of Structures.PLoS computational biology · 2015Article
- Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins.Journal of biomolecular NMR · 2015Article
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4 authors.
Funding
Abstract
A remaining challenge in protein modeling is to predict structures for sequences with no sequence similarity to any experimentally solved structure. Based on earlier observations, the library of protein backbone supersecondary structure motifs (Smotifs) saturated about a decade ago. Therefore, it should be possible to build any structure from a combination of existing Smotifs with the help of limited experimental data that are sufficient to relate the backbone conformations of Smotifs between target proteins and known structures. Here, we present a hybrid modeling algorithm that relies on an exhaustive Smotif library and on nuclear magnetic resonance chemical shift patterns without any input of primary sequence information. In a test of 102 proteins, the algorithm delivered 90 homology-model-quality models, among them 24 high-quality ones, and a topologically correct solution for almost all cases. The current approach opens a venue to address the modeling of larger protein structures for which chemical shifts are available.
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