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1H, 13C and 15N resonance assignment of the SARS-CoV-2 full-length nsp1 protein and its mutants reveals its unique secondary structure features in solution
Tatiana Agback, Francisco Dominguez, Ilya Frolov, Elena I. Frolova, View ORCID ProfilePeter Agback
doi: https://doi.org/10.1101/2021.05.05.442725
Tatiana Agback
1Department of Molecular Sciences, Swedish University of Agricultural Sciences, PO Box 7015, SE-750 07 Uppsala, Sweden
Francisco Dominguez
2Department of Microbiology, University of Alabama at Birmingham, AL, USA
Ilya Frolov
2Department of Microbiology, University of Alabama at Birmingham, AL, USA
Elena I. Frolova
2Department of Microbiology, University of Alabama at Birmingham, AL, USA
Peter Agback
1Department of Molecular Sciences, Swedish University of Agricultural Sciences, PO Box 7015, SE-750 07 Uppsala, Sweden
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Posted May 05, 2021.
1H, 13C and 15N resonance assignment of the SARS-CoV-2 full-length nsp1 protein and its mutants reveals its unique secondary structure features in solution
Tatiana Agback, Francisco Dominguez, Ilya Frolov, Elena I. Frolova, Peter Agback
bioRxiv 2021.05.05.442725; doi: https://doi.org/10.1101/2021.05.05.442725
1H, 13C and 15N resonance assignment of the SARS-CoV-2 full-length nsp1 protein and its mutants reveals its unique secondary structure features in solution
Tatiana Agback, Francisco Dominguez, Ilya Frolov, Elena I. Frolova, Peter Agback
bioRxiv 2021.05.05.442725; doi: https://doi.org/10.1101/2021.05.05.442725
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