ReviewFrontiers in molecular biosciences2018
Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments.
Review in Frontiers in molecular biosciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 19 citations in OpenAlex.
- Semi-synthesis of the C-terminal region ofRSC chemical biology · 2026Article
- An AI-enabled structural atlas decodes kinase specificity across the human proteome.Nature biotechnology · 2026Article
- Purification and preparation of Marchantia polymorpha Auxin Response Factor 2 for phase separation studies.FEBS open bio · 2026Article
- Accessing intractable, phosphorylated intrinsically disordered proteins via a protease-cleavable inclusion body tag.Protein science : a publication of the Protein Society · 2026Article
- A Cysteine-Specific Cationization Strategy for Versatile Antibody Production against Intrinsically Disordered Proteins.Bioconjugate chemistry · 2026Article
- Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12.Nature communications · 2025Article
- Investigating Protein-Protein Interactions of Autophagy-Involved TNIP1.Methods in molecular biology (Clifton, N.J.) · 2025Article
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- Chemical tools for study and modulation of biomolecular phase transitions.Chemical science · 2022Review
- SETDB1-like MET-2 promotes transcriptional silencing and development independently of its H3K9me-associated catalytic activity.Nature structural & molecular biology · 2022Article
- Intrinsically Disordered Proteins (IDP): Purification Under Denaturing Conditions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Facile tethering of stable and unstable proteins for optical tweezers experiments.Biophysical journal · 2021Article
- Article
- The intrinsically disordered region of GCE protein adopts a more fixed structure by interacting with the LBD of the nuclear receptor FTZ-F1.Cell communication and signaling : CCS · 2020Article
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1 author at 1 institution in 1 country.
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Abstract
Intrinsically disordered proteins (IDPs) represent a structural class of proteins that do not have a well-defined, 3D fold in solution, and often have little secondary structure. To characterize their function and molecular mechanism, it is helpful to examine their structure using nuclear magnetic resonance (NMR), which can report on properties, such as residual structure (at both the secondary and tertiary levels), ligand binding affinity, and the effect of ligand binding on IDP structure, all on a per residue basis. This brief review reports on the common problems and decisions that are involved when preparing a disordered protein for NMR studies. The paper covers gene design, expression host choice, protein purification, and the initial NMR experiments that are performed. While many of these steps are essentially identical to those for ordered proteins, a few key differences are highlighted, including the extreme sensitivity of IDPs to proteolytic cleavage, the ability to use denaturing conditions without having to refold the protein, the optimal chromatographic system choice, and the challenges of quantifying an IDP. After successful purification, characterization by NMR can be done using the standard
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