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| Home > Publications database > 1H, 13C, and 15Nresonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A > print |
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| 005 | 20200402210039.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21516467 |
| 024 | 7 | _ | |2 DOI |a 10.1007/s12104-011-9309-2 |
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| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 084 | _ | _ | |2 WoS |a Spectroscopy |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Feuerstein, S. |b 0 |
| 245 | _ | _ | |a 1H, 13C, and 15Nresonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A |
| 260 | _ | _ | |a Dordrecht [u.a.] |b Springer Netherlands |c 2011 |
| 300 | _ | _ | |a 241 - 243 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 18205 |a Biomolecular NMR Assignments |v 5 |x 1874-2718 |y 2 |
| 500 | _ | _ | |a This work was supported by the CEA, the CNRS, the University of Grenoble 1, and the Deutsche Forschungsgemeinschaft (SFB575). We would like to thank Beate Bersch and Adrien Favier (IBS Grenoble) for stimulating discussions. |
| 520 | _ | _ | |a Non-structural protein 5A (NS5A) plays an important role in the life cycle of hepatitis C virus. This proline-rich phosphoprotein is organized into three domains. Besides its role in virus replication and virus assembly, NS5A is involved in a variety of cellular regulation processes. Recent studies on domain 2 and 3 revealed that both belong to the class of intrinsically disordered proteins as they adopt a natively unfolded state. In particular, domain 2 together with its vicinal regions is responsible for NS5A's multiple interactions with other proteins necessary for virus persistence. The low chemical shift dispersion observed for instrinsically disordered proteins presents a challenge for NMR spectroscopy. Here we report sequential resonance assignment of a 179-residue fragment of NS5A, comprising the entire domain 2, using a set of sensitivity and resolution optimized 3D correlation experiments, as well as amino-acid-type editing in (1)H-(15)N correlation spectra. Our assignment reveals the presence of several segments with high propensity to form α-helical structure that may be of importance to the function of this protein fragment as a versatile interaction platform. |
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| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Binding Sites |
| 650 | _ | 2 | |2 MeSH |a Hepacivirus: chemistry |
| 650 | _ | 2 | |2 MeSH |a Isotopes: chemistry |
| 650 | _ | 2 | |2 MeSH |a Nuclear Magnetic Resonance, Biomolecular |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Recombinant Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Viral Nonstructural Proteins: chemistry |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Isotopes |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a NS-5 protein, hepatitis C virus |
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| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Viral Nonstructural Proteins |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a HCV |
| 653 | 2 | 0 | |2 Author |a NS5A |
| 653 | 2 | 0 | |2 Author |a Domain 2 |
| 653 | 2 | 0 | |2 Author |a Heteronuclear NMR |
| 653 | 2 | 0 | |2 Author |a Resonance assignment |
| 653 | 2 | 0 | |2 Author |a Intrinsically disordered proteins |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Solyom, Z. |b 1 |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB58377 |a Aladag, A. |b 2 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB630 |a Hoffmann, S. |b 3 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, D. |b 4 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB101061 |a Brutscher, B. |b 5 |u FZJ |
| 773 | _ | _ | |0 PERI:(DE-600)2388861-1 |a 10.1007/s12104-011-9309-2 |g Vol. 5, p. 241 - 243 |p 241 - 243 |q 5<241 - 243 |t Biomolecular NMR assignments |v 5 |x 1874-2718 |y 2011 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1007/s12104-011-9309-2 |
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| 914 | 1 | _ | |y 2011 |
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