This study characterizes the nucleocapsid (N) protein of SARS-CoV-2 at atomic resolution using solution NMR spectroscopy. A stepwise approach, progressing from the N-terminal domain to the N-terminal region and the full-length protein, reveals the functional role of intrinsically disordered regions in modulating structural dynamics and molecular interactions. Binding studies with low-molecular-weight heparins highlight a ligand length dependent increase in affinity, providing insight into N protein interactions with polyanionic molecules.

NMR investigation of structural heterogeneity and ligand recognition in the SARS-COV-2 nucleocapsid protein / Tessa Bolognesi, Marco Schiavina, Cristina Ciabini, Stefano Elli, Michela Parafioriti, Marco Guerrini, Isabella C. Felli, Roberta Pierattelli. - ELETTRONICO. - (2026), pp. 0-0. ( ITACA.SB "Integrative Structural Biology Meeting" 2026).

NMR investigation of structural heterogeneity and ligand recognition in the SARS-COV-2 nucleocapsid protein

Tessa Bolognesi;Marco Schiavina;Cristina Ciabini;Isabella C. Felli;Roberta Pierattelli
2026

Abstract

This study characterizes the nucleocapsid (N) protein of SARS-CoV-2 at atomic resolution using solution NMR spectroscopy. A stepwise approach, progressing from the N-terminal domain to the N-terminal region and the full-length protein, reveals the functional role of intrinsically disordered regions in modulating structural dynamics and molecular interactions. Binding studies with low-molecular-weight heparins highlight a ligand length dependent increase in affinity, providing insight into N protein interactions with polyanionic molecules.
2026
Book of abstract ITACA.SB "Integrative Structural Biology Meeting" 2026
ITACA.SB "Integrative Structural Biology Meeting" 2026
Tessa Bolognesi, Marco Schiavina, Cristina Ciabini, Stefano Elli, Michela Parafioriti, Marco Guerrini, 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/2158/1459333
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