ArticleAnalytical biochemistry2014
Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods.
Article in Analytical biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 49 citations in OpenAlex.
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- Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Acetylation-Dependent Compaction of the Histone H4 Tail Ensemble.The journal of physical chemistry. B · 2024Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.bioRxiv : the preprint server for biology · 2024Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
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- A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins.Frontiers in molecular biosciences · 2022Article
- Cell Cycle Regulation of the Pdx1 Transcription Factor in Developing Pancreas and Insulin-Producing β-Cells.Diabetes · 2021Article
- Characterization of functional disordered regions within chromatin-associated proteins.iScience · 2021Review
- Novel NMR Assignment Strategy Reveals Structural Heterogeneity in Solution of the nsP3 HVD Domain of Venezuelan Equine Encephalitis Virus.Molecules (Basel, Switzerland) · 2020Article
- HACANCOi: a new HJournal of biomolecular NMR · 2020Article
- Dispersion from CJournal of biomolecular NMR · 2020Article
- Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action.Biophysical journal · 2019Article
- A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain.Structure (London, England : 1993) · 2019Article
- Solution Ensemble of the C-Terminal Domain from the Transcription Factor Pdx1 Resembles an Excluded Volume Polymer.The journal of physical chemistry. B · 2019Article
- Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments.Molecular cell · 2018Article
- The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3.Biophysical journal · 2018Article
- Direct detection of carbon and nitrogen nuclei for high-resolution analysis of intrinsically disordered proteins using NMR spectroscopy.Methods (San Diego, Calif.) · 2018Article
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3 authors at 1 institution in 1 country.
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Abstract
There is an extraordinary need to describe the structures of intrinsically disordered proteins (IDPs) due to their role in various biological processes involved in signaling and transcription. However, general study of IDPs by NMR spectroscopy is limited by the poor (1)H amide chemical shift dispersion typically observed in their spectra. Recently, (13)C direct-detected NMR spectroscopy has been recognized as enabling broad structural study of IDPs. Most notably, multidimensional experiments based on the (15)N,(13)C CON spectrum make complete chemical shift assignment feasible. Here we document a collection of NMR-based tools that efficiently lead to chemical shift assignment of IDPs, motivated by a case study of the C-terminal disordered region from the human pancreatic transcription factor Pdx1. Our strategy builds on the combination of two three-dimensional (3D) experiments, (HN-flip)N(CA)CON and 3D (HN-flip)N(CA)NCO, that enable daisy chain connections to be built along the IDP backbone, facilitated by acquisition of amino acid-specific (15)N,(13)C CON-detected experiments. Assignments are completed through carbon-detected, total correlation spectroscopy (TOCSY)-based side chain chemical shift measurement. Conducting our study required producing valuable modifications to many previously published pulse sequences, motivating us to announce the creation of a database of our pulse programs, which we make freely available through our website.
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