Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis
(2021) In Magnetic Resonance 2(1). p.129-138- Abstract
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/d0440703-feee-4b82-bd97-2972767d3b16
- author
- Robertson, Angus J. LU ; Ying, Jinfa and Bax, Ad
- publishing date
- 2021-04-13
- type
- Contribution to journal
- publication status
- published
- in
- Magnetic Resonance
- volume
- 2
- issue
- 1
- pages
- 129 - 138
- publisher
- Copernicus GmbH
- external identifiers
-
- scopus:85119347905
- ISSN
- 2699-0016
- DOI
- 10.5194/mr-2-129-2021
- language
- English
- LU publication?
- no
- id
- d0440703-feee-4b82-bd97-2972767d3b16
- date added to LUP
- 2024-01-25 15:46:35
- date last changed
- 2024-01-26 14:11:46
@article{d0440703-feee-4b82-bd97-2972767d3b16, abstract = {{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.}}, author = {{Robertson, Angus J. and Ying, Jinfa and Bax, Ad}}, issn = {{2699-0016}}, language = {{eng}}, month = {{04}}, number = {{1}}, pages = {{129--138}}, publisher = {{Copernicus GmbH}}, series = {{Magnetic Resonance}}, title = {{Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis}}, url = {{http://dx.doi.org/10.5194/mr-2-129-2021}}, doi = {{10.5194/mr-2-129-2021}}, volume = {{2}}, year = {{2021}}, }