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dc.contributor.author
Callon, Morgane
dc.contributor.author
Luder, Dominique
dc.contributor.author
Malär, Alexander A.
dc.contributor.author
Wiegand, Thomas
dc.contributor.author
Rimal, Vaclav
dc.contributor.author
Lecoq, Lauriane
dc.contributor.author
Böckmann, Anja
dc.contributor.author
Samoson, Ago
dc.contributor.author
Meier, Beat H.
dc.date.accessioned
2023-10-24T08:43:21Z
dc.date.available
2023-10-05T03:44:15Z
dc.date.available
2023-10-06T06:46:07Z
dc.date.available
2023-10-24T08:43:21Z
dc.date.issued
2023-10-21
dc.identifier.issn
2041-6520
dc.identifier.issn
2041-6539
dc.identifier.other
10.1039/d3sc03539e
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/635029
dc.identifier.doi
10.3929/ethz-b-000635029
dc.description.abstract
The NMR spectra of side-chain protons in proteins provide important information, not only about their structure and dynamics, but also about the mechanisms that regulate interactions between macromolecules. However, in the solid-state, these resonances are particularly difficult to resolve, even in relatively small proteins. We show that magic-angle-spinning (MAS) frequencies of 160 kHz, combined with a high magnetic field of 1200 MHz proton Larmor frequency, significantly improve their spectral resolution. We investigate in detail the gain for MAS frequencies between 110 and 160 kHz MAS for a model sample as well as for the hepatitis B viral capsid assembled from 120 core-protein (Cp) dimers. For both systems, we found a significantly improved spectral resolution of the side-chain region in the ¹H–¹³C 2D spectra. The combination of 160 kHz MAS frequency with a magnetic field of 1200 MHz, allowed us to assign 61% of the aliphatic protons of Cp. The side-chain proton assignment opens up new possibilities for structural studies and further characterization of protein–protein or protein–nucleic acid interactions.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Royal Society of Chemistry
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/3.0/
dc.title
High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 3.0 Unported
dc.date.published
2023-09-20
ethz.journal.title
Chemical Science
ethz.journal.volume
14
en_US
ethz.journal.issue
39
en_US
ethz.journal.abbreviated
Chem. Sci.
ethz.pages.start
10824
en_US
ethz.pages.end
10834
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
NMR studies in the Solid State
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.grant.agreementno
188711
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
Projekte MINT
ethz.date.deposited
2023-10-05T03:44:18Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2024-02-03T05:40:50Z
ethz.rosetta.lastUpdated
2024-02-03T05:40:50Z
ethz.rosetta.versionExported
true
ethz.COinS
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