Cargando…
NMR Observation of Sulfhydryl Signals in SARS‐CoV‐2 Main Protease Aids Structural Studies
The 68‐kDa homodimeric 3C‐like protease of SARS‐CoV‐2, M(pro) (3CL(pro)/Nsp5), is a key antiviral drug target. NMR spectroscopy of this large system proved challenging and resonance assignments have remained incomplete. Here we present the near‐complete (>97 %) backbone assignments of a C145A var...
Autores principales: | Robertson, Angus J., Ying, Jinfa, Bax, Ad |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9537880/ https://www.ncbi.nlm.nih.gov/pubmed/35972230 http://dx.doi.org/10.1002/cbic.202200471 |
Ejemplares similares
-
Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis
por: Robertson, Angus J., et al.
Publicado: (2021) -
Concordance
of X-ray and AlphaFold2 Models
of SARS-CoV-2 Main Protease with Residual Dipolar Couplings Measured in Solution
por: Robertson, Angus J., et al.
Publicado: (2021) -
Validation of X-ray Crystal Structure Ensemble Representations of SARS-CoV-2 Main Protease by Solution NMR Residual Dipolar Couplings
por: Shen, Yang, et al.
Publicado: (2023) -
Imino Hydrogen Positions
in Nucleic Acids from Density
Functional Theory Validated by NMR Residual Dipolar Couplings
por: Grishaev, Alexander, et al.
Publicado: (2012) -
Activation and maturation of SARS-CoV main protease
por: Xia, Bin, et al.
Publicado: (2011)