ArticleCommunications biology2022
Validated determination of NRG1 Ig-like domain structure by mass spectrometry coupled with computational modeling.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 14 citations in OpenAlex.
- Comprehensive Tutorial for Computational Methods of Protein Structure Prediction Incorporating Mass Spectrometry Data.Mass spectrometry reviews · 2026Review
- Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.Nature methods · 2026Review
- Multidose Inline Size-Exclusion Chromatography-Flash Oxidation for Structural Analysis of Dynamic Protein-Ligand Interactions of Antithrombin III and Unfractionated Heparin.Analytical chemistry · 2026Article
- Ion Mobility Mass Spectrometry Guided Modeling with AlphaFold and Rosetta Improves Protein Complex Structure Prediction.bioRxiv : the preprint server for biology · 2026Article
- Deep-learning structure elucidation from single-mutant deep mutational scanning.Nature communications · 2025Article
- Systematic Fe(II)-EDTA Method of Dose-Dependent Hydroxyl Radical Generation for Protein Oxidative Footprinting.Analytical chemistry · 2023Article
- Dimethylthiourea as a Quencher in Hydroxyl Radical Protein Footprinting Experiments.Journal of the American Society for Mass Spectrometry · 2023Article
- 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
- Application of Multiple Length Cross-linkers to the Characterization of Gaseous Protein Structure.Analytical chemistry · 2022Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
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Abstract
High resolution hydroxyl radical protein footprinting (HR-HRPF) is a mass spectrometry-based method that measures the solvent exposure of multiple amino acids in a single experiment, offering constraints for experimentally informed computational modeling. HR-HRPF-based modeling has previously been used to accurately model the structure of proteins of known structure, but the technique has never been used to determine the structure of a protein of unknown structure. Here, we present the use of HR-HRPF-based modeling to determine the structure of the Ig-like domain of NRG1, a protein with no close homolog of known structure. Independent determination of the protein structure by both HR-HRPF-based modeling and heteronuclear NMR was carried out, with results compared only after both processes were complete. The HR-HRPF-based model was highly similar to the lowest energy NMR model, with a backbone RMSD of 1.6 Å. To our knowledge, this is the first use of HR-HRPF-based modeling to determine a previously uncharacterized protein structure.
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