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000016572 0247_ $$2pmid$$apmid:21516467
000016572 0247_ $$2DOI$$a10.1007/s12104-011-9309-2
000016572 0247_ $$2WOS$$aWOS:000294559700027
000016572 037__ $$aPreJuSER-16572
000016572 041__ $$aeng
000016572 082__ $$a570
000016572 084__ $$2WoS$$aBiophysics
000016572 084__ $$2WoS$$aSpectroscopy
000016572 1001_ $$0P:(DE-HGF)0$$aFeuerstein, S.$$b0
000016572 245__ $$a1H, 13C, and 15Nresonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A
000016572 260__ $$aDordrecht [u.a.]$$bSpringer Netherlands$$c2011
000016572 300__ $$a241 - 243
000016572 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000016572 3367_ $$00$$2EndNote$$aJournal Article
000016572 3367_ $$2BibTeX$$aARTICLE
000016572 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000016572 3367_ $$2DRIVER$$aarticle
000016572 440_0 $$018205$$aBiomolecular NMR Assignments$$v5$$x1874-2718$$y2
000016572 500__ $$aThis work was supported by the CEA, the CNRS, the University of Grenoble 1, and the Deutsche Forschungsgemeinschaft (SFB575). We would like to thank Beate Bersch and Adrien Favier (IBS Grenoble) for stimulating discussions.
000016572 520__ $$aNon-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.
000016572 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000016572 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000016572 588__ $$aDataset connected to Web of Science, Pubmed
000016572 65320 $$2Author$$aHCV
000016572 65320 $$2Author$$aNS5A
000016572 65320 $$2Author$$aDomain 2
000016572 65320 $$2Author$$aHeteronuclear NMR
000016572 65320 $$2Author$$aResonance assignment
000016572 65320 $$2Author$$aIntrinsically disordered proteins
000016572 650_2 $$2MeSH$$aBinding Sites
000016572 650_2 $$2MeSH$$aHepacivirus: chemistry
000016572 650_2 $$2MeSH$$aIsotopes: chemistry
000016572 650_2 $$2MeSH$$aNuclear Magnetic Resonance, Biomolecular
000016572 650_2 $$2MeSH$$aProtein Conformation
000016572 650_2 $$2MeSH$$aProtein Structure, Tertiary
000016572 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000016572 650_2 $$2MeSH$$aViral Nonstructural Proteins: chemistry
000016572 650_7 $$00$$2NLM Chemicals$$aIsotopes
000016572 650_7 $$00$$2NLM Chemicals$$aNS-5 protein, hepatitis C virus
000016572 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000016572 650_7 $$00$$2NLM Chemicals$$aViral Nonstructural Proteins
000016572 650_7 $$2WoSType$$aJ
000016572 7001_ $$0P:(DE-HGF)0$$aSolyom, Z.$$b1
000016572 7001_ $$0P:(DE-Juel1)VDB58377$$aAladag, A.$$b2$$uFZJ
000016572 7001_ $$0P:(DE-Juel1)VDB630$$aHoffmann, S.$$b3$$uFZJ
000016572 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000016572 7001_ $$0P:(DE-Juel1)VDB101061$$aBrutscher, B.$$b5$$uFZJ
000016572 773__ $$0PERI:(DE-600)2388861-1$$a10.1007/s12104-011-9309-2$$gVol. 5, p. 241 - 243$$p241 - 243$$q5<241 - 243$$tBiomolecular NMR assignments$$v5$$x1874-2718$$y2011
000016572 8567_ $$uhttp://dx.doi.org/10.1007/s12104-011-9309-2
000016572 909CO $$ooai:juser.fz-juelich.de:16572$$pVDB
000016572 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer review
000016572 9141_ $$y2011
000016572 9131_ $$0G:(DE-Juel1)FUEK409$$aDE-HGF$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000016572 9131_ $$0G:(DE-Juel1)FUEK505$$aDE-HGF$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000016572 9132_ $$0G:(DE-HGF)POF3-553$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft  Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vPhysical Basis of Diseases$$x0
000016572 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$gICS$$kICS-6$$lStrukturbiochemie$$x0
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