Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis

Robertson, Angus J.; Ying, Jinfa; Bax, Ad

Resonance assignment and structural studies of larger proteins by nuclear magnetic resonance (NMR) can be challenging when exchange broadening, multiple stable conformations, and inline-formula1H back-exchange of the fully deuterated chain pose problems. These difficulties arise for the SARS-CoV-2 Main Protease, a homodimer of 2 inline-formula× 306 residues. We demonstrate that the combination of four-dimensional (4D) TROSY-NOESY-TROSY spectroscopy and 4D NOESY-NOESY-TROSY spectroscopy provides an effective tool for delineating the inline-formula1H–inline-formula1H dipolar relaxation network. In combination with detailed structural information obtained from prior X-ray crystallography work, such data are particularly useful for extending and validating resonance assignments as well as for probing structural features.

Zitieren

Zitierform:

Robertson, Angus J. / Ying, Jinfa / Bax, Ad: Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis. 2021. Copernicus Publications.

Zugriffsstatistik

Gesamt:
Volltextzugriffe:
Metadatenansicht:
12 Monate:
Volltextzugriffe:
Metadatenansicht:

Grafik öffnen

Rechte

Rechteinhaber: Angus J. Robertson et al.

Nutzung und Vervielfältigung:

Export