The SARS-CoV-2 Nucleocapsid (N) protein is a 419-amino-acid multidomain protein involved in viral RNA packaging. It includes structured domains (NTD, CTD) and three intrinsically disordered regions (IDRs). This study focuses on characterizing the full-length (FL) N protein and its RNA interaction, comparing it to simpler constructs like NTD and NTR. Previous studies show that IDRs enhance RNA binding. The full-length dimeric form is expected to further increase affinity via synergistic effects. We report recent findings on FL N, including its expression, purification, and structural analysis via NMR.

Expression of the Nucleocapsid Protein (N) from SARS-CoV 2 and its Characterization through High-Field NMR Spectroscopy / Tessa Bolognesi, Marco Schiavina, Isabella C. Felli, Roberta Pierattelli. - ELETTRONICO. - (2024), pp. 1-1. ( XXVIII National Congress SCI 2024).

Expression of the Nucleocapsid Protein (N) from SARS-CoV 2 and its Characterization through High-Field NMR Spectroscopy

Tessa Bolognesi;Marco Schiavina;Isabella C. Felli;Roberta Pierattelli
2024

Abstract

The SARS-CoV-2 Nucleocapsid (N) protein is a 419-amino-acid multidomain protein involved in viral RNA packaging. It includes structured domains (NTD, CTD) and three intrinsically disordered regions (IDRs). This study focuses on characterizing the full-length (FL) N protein and its RNA interaction, comparing it to simpler constructs like NTD and NTR. Previous studies show that IDRs enhance RNA binding. The full-length dimeric form is expected to further increase affinity via synergistic effects. We report recent findings on FL N, including its expression, purification, and structural analysis via NMR.
2024
Book of abstracts SCI 2024
XXVIII National Congress SCI 2024
Tessa Bolognesi, Marco Schiavina, Isabella C. Felli, Roberta Pierattelli
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1431103
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