Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Robertson, Angus J. LU ; Ying, Jinfa and Bax, Ad (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:
author
; and
publishing date
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}},
}