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- W3142548340 abstract "<strong class=journal-contentHeaderColor>Abstract.</strong> Resonance assignment and structural studies of larger proteins by nuclear magnetic resonance (NMR) can be challenging when exchange broadening, multiple stable conformations, and <span class=inline-formula><sup>1</sup></span>H back-exchange of the fully deuterated chain pose problems. These difficulties arise for the SARS-CoV-2 Main Protease, a homodimer of 2â<span class=inline-formula>Ã</span>â306 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 <span class=inline-formula><sup>1</sup></span>Hâ<span class=inline-formula><sup>1</sup></span>H 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." @default.
- W3142548340 created "2021-04-13" @default.
- W3142548340 creator A5082289559 @default.
- W3142548340 date "2021-03-26" @default.
- W3142548340 modified "2023-10-03" @default.
- W3142548340 title "Comment on mr-2021-19" @default.
- W3142548340 doi "https://doi.org/10.5194/mr-2021-19-ac1" @default.
- W3142548340 hasPublicationYear "2021" @default.
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