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10.1007/s12104-021-10009-8

http://scihub22266oqcxt.onion/10.1007/s12104-021-10009-8
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suck abstract from ncbi


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pmid33660218      Biomol+NMR+Assign 2021 ; 15 (1): 219-227
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  • The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR #MMPMID33660218
  • Schiavina M; Pontoriero L; Uversky VN; Felli IC; Pierattelli R
  • Biomol NMR Assign 2021[Apr]; 15 (1): 219-227 PMID33660218show ga
  • The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure as can be inferred by bioinformatics analyses as well as from the data available for the homologous protein from SARS-CoV. The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1-248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein.
  • |*Magnetic Resonance Spectroscopy[MESH]
  • |Carbon Isotopes[MESH]
  • |Computational Biology[MESH]
  • |Coronavirus Nucleocapsid Proteins/*chemistry[MESH]
  • |Hydrogen[MESH]
  • |Nitrogen Isotopes[MESH]
  • |Phosphoproteins/chemistry[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |Protein Structure, Secondary[MESH]


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