| Autor: |
A. J. Robertson, J. Ying, A. Bax |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
Magnetic Resonance, Vol 2, Pp 129-138 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2699-0016 |
| DOI: |
10.5194/mr-2-129-2021 |
| Popis: |
Resonance assignment and structural studies of larger proteins by nuclear magnetic resonance (NMR) can be challenging when exchange broadening, multiple stable conformations, and 1H back-exchange of the fully deuterated chain pose problems. These difficulties arise for the SARS-CoV-2 Main Protease, a homodimer of 2 × 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 1H–1H 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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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