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Updated: Nov 11, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9
Erika F Dudás1, Rita Puglisi1, Sophie Marianne Korn2,3
1Department of Basic and Clinical Neuroscience, Maurice Wohl Institute, UK-DRI at King's College London, 5 Cutcombe Rd, London, SE59RT, UK.
Abstract:
As part of an International consortium aiming at the characterization by NMR of the proteins of the SARS-CoV-2 virus, we have obtained the virtually complete assignment of the backbone atoms of the non-structural protein nsp9. This small (12 kDa) protein is encoded by ORF1a, binds to RNA and seems to be essential for viral RNA synthesis. The crystal structures of the SARS-CoV-2 protein and other homologues suggest that the protein is dimeric as also confirmed by analytical ultracentrifugation and dynamic light scattering. Our data constitute the prerequisite for further NMR-based characterization, and provide the starting point for the identification of small molecule lead compounds that could interfere with RNA binding and prevent viral replication.
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