Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 15, Issue 1, Pages 219-227Publisher
SPRINGER
DOI: 10.1007/s12104-021-10009-8
Keywords
SARS-CoV-2; Covid-19; Nucleocapsid protein; NMR spectroscopy; C-13 detection; IDPs
Categories
Funding
- Universita degli Studi di Firenze within the CRUI-CARE Agreement
- Fondazione CR Firenze
- Italian Ministry for University and Research
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The study focuses on the nucleocapsid protein N from SARS-CoV-2, specifically the 1-248 construct, and reports the sequence-specific assignment of two disordered regions within this protein. This is a significant step towards the complete characterization of the protein.
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.
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