ArticleProtein science : a publication of the Protein Society2021
NMR hawk-eyed view of AlphaFold2 structures.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 50 citations in OpenAlex.
- Hidden structural states of proteins revealed by conformer selection.Nature communications · 2026Article
- Rescuing fertility: C-Phycocyanin prevents ovarian damage through NRF2-mediated ferroptosis pathways in polycystic ovary syndrome models.Zoological research · 2025Article
- Leveraging AlphaFold2 and residual dipolar couplings for side-chain methyl group assignment: A case study with S. cerevisiae Xrs2.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Critical Assessment of RNA and DNA Structure Predictions via Artificial Intelligence: The Imitation Game.Journal of chemical information and modeling · 2025Article
- The power and pitfalls of AlphaFold2 for structure prediction beyond rigid globular proteins.Nature chemical biology · 2024Review
- A druggable conformational switch in the c-MYC transactivation domain.Nature communications · 2024Article
- Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dynamic Evolution of Bacterial Ligand Recognition by Formyl Peptide Receptors.Genome biology and evolution · 2023Article
- Experimental NOE, Chemical Shift, and Proline Isomerization Data Provide Detailed Insights into Amelotin Oligomerization.Journal of the American Chemical Society · 2023Article
- Blind assessment of monomeric AlphaFold2 protein structure models with experimental NMR data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Solution Structure Ensembles of the Open and Closed Forms of the ∼130 kDa Enzyme I via AlphaFold Modeling, Coarse Grained Simulations, and NMR.Journal of the American Chemical Society · 2023Article
- Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023Review
- Recombinant Expression and Chemical Amidation of Isotopically Labeled Native Melittin.Journal of the American Chemical Society · 2023Article
- A "grappling hook" interaction connects self-assembly and chaperone activity of Nucleophosmin 1.PNAS nexus · 2023Article
- Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation.Biochemical Society transactions · 2022Review
- Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022Review
- Molecular Characterization and SNP-Based Molecular Marker Development of Two Novel High Molecular Weight Glutenin Genes fromInternational journal of molecular sciences · 2022Article
- The accuracy of protein structures in solution determined by AlphaFold and NMR.Structure (London, England : 1993) · 2022Article
- Complementing machine learning-based structure predictions with native mass spectrometry.Protein science : a publication of the Protein Society · 2022Article
- The AlphaFold Database of Protein Structures: A Biologist's Guide.Journal of molecular biology · 2022Review
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1 author at 1 institution in 1 country.
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Abstract
The prediction of the three-dimensional (3D) structure of proteins from the amino acid sequence made a stunning breakthrough reaching atomic accuracy. Using the neural network-based method AlphaFold2, 3D structures of almost the entire human proteome have been predicted and made available (https://www.alphafold.ebi.ac.uk). To gain insight into how well AlphaFold2 structures represent the conformation of proteins in solution, I here compare the AlphaFold2 structures of selected small proteins with their 3D structures that were determined by nuclear magnetic resonance (NMR) spectroscopy. Proteins were selected for which the 3D solution structures were determined on the basis of a very large number of distance restraints and residual dipolar couplings and are thus some of the best-resolved solution structures of proteins to date. The quality of the backbone conformation of the AlphaFold2 structures is assessed by fitting a large set of experimental residual dipolar couplings (RDCs). The analysis shows that experimental RDCs fit extremely well to the AlphaFold2 structures predicted for GB3, DinI, and ubiquitin. In the case of GB3, the accuracy of the AlphaFold2 structure even surpasses that of a 1.1 Å crystal structure. Fitting of experimental RDCs furthermore allows identification of AlphaFold2 structures that are best representative of the protein's conformation in solution as seen for the EF hands of the N-terminal domain of Ca
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