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dc.contributor.author
Lecoq, Lauriane
dc.contributor.author
Fogeron, Marie-Laure
dc.contributor.author
Meier, Beat H.
dc.contributor.author
Nassal, Michael
dc.contributor.author
Böckmann, Anja
dc.date.accessioned
2020-10-13T08:46:21Z
dc.date.available
2020-10-11T05:17:46Z
dc.date.available
2020-10-13T08:46:21Z
dc.date.issued
2020-10
dc.identifier.issn
1999-4915
dc.identifier.other
10.3390/v12101069
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/445431
dc.identifier.doi
10.3929/ethz-b-000445431
dc.description.abstract
Structural virology reveals the architecture underlying infection. While notably electron microscopy images have provided an atomic view on viruses which profoundly changed our understanding of these assemblies incapable of independent life, spectroscopic techniques like NMR enter the field with their strengths in detailed conformational analysis and investigation of dynamic behavior. Typically, the large assemblies represented by viral particles fall in the regime of biological high-resolution solid-state NMR, able to follow with high sensitivity the path of the viral proteins through their interactions and maturation steps during the viral life cycle. We here trace the way from first solid-state NMR investigations to the state-of-the-art approaches currently developing, including applications focused on HIV, HBV, HCV and influenza, and an outlook to the possibilities opening in the coming years.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
MDPI
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
structure
en_US
dc.subject
solid-state NMR
en_US
dc.subject
viral proteins
en_US
dc.subject
capsids
en_US
dc.subject
membrane proteins
en_US
dc.title
Solid-state NMR for studying the structure and dynamics of viral assemblies
en_US
dc.type
Review Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2020-09-24
ethz.journal.title
Viruses
ethz.journal.volume
12
en_US
ethz.journal.issue
10
en_US
ethz.pages.start
1069
en_US
ethz.size
26 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Basel
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02543 - Inst. f. Molekulare Physikalische Wiss. / Institute of Molecular Physical Science::03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02543 - Inst. f. Molekulare Physikalische Wiss. / Institute of Molecular Physical Science::03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
ethz.date.deposited
2020-10-11T05:17:51Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2020-10-13T08:46:34Z
ethz.rosetta.lastUpdated
2024-02-02T12:17:58Z
ethz.rosetta.versionExported
true
ethz.COinS
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