ArticleProtein science : a publication of the Protein Society2012
Detection of disordered regions in globular proteins using ¹³C-detected NMR.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Article
- Ligand accessibility to heme cytochrome bJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase.Scientific reports · 2018Article
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.Nature communications · 2016Article
- CP-HISQC: a better version of HSQC experiment for intrinsically disordered proteins under physiological conditions.Journal of biomolecular NMR · 2014Article
- Challenges and opportunities in targeting the menin-MLL interaction.Future medicinal chemistry · 2014Review
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Authors and funding
4 authors.
Funding
Abstract
Characterization of disordered regions in globular proteins constitutes a significant challenge. Here, we report an approach based on ¹³C-detected nuclear magnetic resonance experiments for the identification and assignment of disordered regions in large proteins. Using this method, we demonstrate that disordered fragments can be accurately identified in two homologs of menin, a globular protein with a molecular weight over 50 kDa. Our work provides an efficient way to characterize disordered fragments in globular proteins for structural biology applications.
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Registered trials
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