ArticleJournal of biomolecular NMR2014
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins.
Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- HACANCOi: a new HJournal of biomolecular NMR · 2020Article
- α-Synuclein in Parkinson's disease: causal or bystander?Journal of neural transmission (Vienna, Austria : 1996) · 2019Review
- Article
- Liquid-liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau.Nature communications · 2017Article
- Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein.Journal of biomolecular NMR · 2016Article
- NMR Meets Tau: Insights into Its Function and Pathology.Biomolecules · 2016Review
- Six- and seven-dimensional experiments by combination of sparse random sampling and projection spectroscopy dedicated for backbone resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2015Article
- (13)C-detected NMR experiments for automatic resonance assignment of IDPs and multiple-fixing SMFT processing.Journal of biomolecular NMR · 2015Article
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3 authors.
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Abstract
Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY) experiment for backbone assignment of intrinsically disordered proteins. The 6D HCACONCAH APSY correlates the six different chemical shifts, H(α)(i - 1), C(α)(i - 1), C'(i - 1), N(i), Cα(i) and Hα(i). Application to two intrinsically disordered proteins, 140-residue α-synuclein and a 352-residue isoform of Tau, demonstrates that the chemical shift information provided by the 6D HCACONCAH APSY allows efficient backbone resonance assignment of intrinsically disordered proteins.
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