ArticleStructure (London, England : 1993)2012
Blind testing of routine, fully automated determination of protein structures from NMR data.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Top-Down Scoring of Spectral Fitness by Image Analysis for Protein Structure Validation.Journal of chemical information and modeling · 2026Article
- Perspective: on the importance of extensive, high-quality and reliable deposition of biomolecular NMR data in the age of artificial intelligence.Journal of biomolecular NMR · 2024Article
- Blind assessment of monomeric AlphaFold2 protein structure models with experimental NMR data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Blind Assessment of Monomeric AlphaFold2 Protein Structure Models with Experimental NMR Data.bioRxiv : the preprint server for biology · 2023Article
- AlphaFold Models of Small Proteins Rival the Accuracy of Solution NMR Structures.Frontiers in molecular biosciences · 2022Article
- Modulating Enzyme FunctionFrontiers in molecular biosciences · 2021Article
- Article
- Combining Evolutionary Covariance and NMR Data for Protein Structure Determination.Methods in enzymology · 2019Article
- AutomaticJournal of biomolecular NMR · 2018Article
- Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins.Journal of biomolecular NMR · 2018Article
- Peak picking multidimensional NMR spectra with the contour geometry based algorithm CYPICK.Journal of biomolecular NMR · 2017Article
- NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.The FEBS journal · 2016Article
- A protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Journal of biomolecular NMR · 2016Article
- Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Automated protein structure determination by NMR.Journal of biomolecular NMR · 2015Article
- NMR data-driven structure determination using NMR-I-TASSER in the CASD-NMR experiment.Journal of biomolecular NMR · 2015Article
- Combined automated NOE assignment and structure calculation with CYANA.Journal of biomolecular NMR · 2015Article
- Improved reliability, accuracy and quality in automated NMR structure calculation with ARIA.Journal of biomolecular NMR · 2015Article
- CASD-NMR 2: robust and accurate unsupervised analysis of raw NOESY spectra and protein structure determination with UNIO.Journal of biomolecular NMR · 2015Article
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37 authors.
Funding
Abstract
The protocols currently used for protein structure determination by nuclear magnetic resonance (NMR) depend on the determination of a large number of upper distance limits for proton-proton pairs. Typically, this task is performed manually by an experienced researcher rather than automatically by using a specific computer program. To assess whether it is indeed possible to generate in a fully automated manner NMR structures adequate for deposition in the Protein Data Bank, we gathered 10 experimental data sets with unassigned nuclear Overhauser effect spectroscopy (NOESY) peak lists for various proteins of unknown structure, computed structures for each of them using different, fully automatic programs, and compared the results to each other and to the manually solved reference structures that were not available at the time the data were provided. This constitutes a stringent "blind" assessment similar to the CASP and CAPRI initiatives. This study demonstrates the feasibility of routine, fully automated protein structure determination by NMR.
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