Dynamics of the Intrinsically Disordered C-Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy

We provide an atomic‐resolution description based on NMR spectroscopy, of the intrinsically disordered C‐terminal domain of the Nipah virus nucleoprotein (NTAIL), both in its isolated state and within the nucleocapsid (NC). Within the NC the second half of NTAIL retains conformational behavior simil...

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Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2015-01, Vol.16 (2), p.268-276
Hauptverfasser:	Baronti, Lorenzo, Erales, Jenny, Habchi, Johnny, Felli, Isabella C., Pierattelli, Roberta, Longhi, Sonia
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Biochemistry, Molecular Biology Hendra virus intrinsically disordered proteins Life Sciences Magnetic Resonance Spectroscopy Models, Molecular Nipah virus Nipah Virus - chemistry NMR NMR spectroscopy Nuclear magnetic resonance Nucleocapsid Proteins - chemistry Nucleocapsid Proteins - metabolism Nucleoproteins - chemistry Nucleoproteins - metabolism Phosphoproteins - chemistry Phosphoproteins - metabolism Protein Conformation Protein Structure, Tertiary protein-protein interactions Quantitative Methods sequence determination Spectrum analysis Structural Biology viral proteins Viral Proteins - chemistry Viral Proteins - metabolism
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