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Article

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.

PloS one - 1 Jan 2021

Agback Tatiana, Dominguez Francisco, Frolov Ilya, Frolova Elena I, Agback Peter

Abstract excerpt

Structural characterization of the SARS-CoV-2 full length nsp1 protein will be an essential tool for developing new target-directed antiviral drugs against SARS-CoV-2 and for further understanding of intra- and intermolecular interactions of this protein. As a first step in the NMR studies of the protein, we report the 1H, 13C and 15N resonance backbone assignment as well as the Cβ of the apo form of the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 34874953
DOI: 10.1371/journal.pone.0251834
PMCID: PMC8651119

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