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.| File | Dimensione | Formato | |
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