ArticleJournal of biomolecular NMR2014
"CON-CON" assignment strategy for highly flexible 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 17 papers.
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17 citing papers in PubMed.
- Integrating molecular dynamics simulation with small- and wide-angle X-ray scattering to unravel the flexibility, antigen-blocking, and protease-restoring functions in a hindrance-based pro-antibody.Protein science : a publication of the Protein Society · 2024Article
- A call to order: Examining structured domains in biomolecular condensates.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Review
- Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.Scientific reports · 2020Article
- A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.Journal of biomolecular NMR · 2018Article
- POTENCI: prediction of temperature, neighbor and pH-corrected chemical shifts for intrinsically disordered proteins.Journal of biomolecular NMR · 2018Article
- Article
- Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.Scientific reports · 2017Article
- Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data.Journal of biomolecular NMR · 2017Article
- Increasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift Reagent.Angewandte Chemie (International ed. in English) · 2016Article
- Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein.Journal of biomolecular NMR · 2016Article
- Sequence Context Influences the Structure and Aggregation Behavior of a PolyQ Tract.Biophysical journal · 2016Article
- Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2016Article
- Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.Biophysical journal · 2016Article
- 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
- HN-NCA heteronuclear TOCSY-NH experiment for (1)H(N) and (15)N sequential correlations in ((13)C, (15)N) labelled 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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9 authors.
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Abstract
Intrinsically disordered proteins (IDPs) are a class of highly flexible proteins whose characterization by NMR spectroscopy is complicated by severe spectral overlaps. The development of experiments designed to facilitate the sequence-specific assignment procedure is thus very important to improve the tools for the characterization of IDPs and thus to be able to focus on IDPs of increasing size and complexity. Here, we present and describe the implementation of a set of novel ¹H-detected 5D experiments, (HACA)CON(CACO)NCO(CA)HA, BT-(H)NCO(CAN)CONNH and BT-HN(COCAN)CONNH, optimized for the study of highly flexible IDPs that exploit the best resolved correlations, those involving the carbonyl and nitrogen nuclei of neighboring amino acids, to achieve sequence-specific resonance assignment. Together with the analogous recently proposed pulse schemes based on ¹³C detection, they form a complete set of experiments for sequence-specific assignment of highly flexible IDPs. Depending on the particular sample conditions (concentration, lifetime, pH, temperature, etc.), these experiments present certain advantages and disadvantages that will be discussed. Needless to say, that the availability of a variety of complementary experiments will be important for accurate determination of resonance frequencies in complex IDPs.
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