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dc.contributor.author
Marchand, Adrien
dc.contributor.author
Czar, Martin F.
dc.contributor.author
Eggel, Elija N.
dc.contributor.author
Kaeslin, Jérôme
dc.contributor.author
Zenobi, Renato
dc.date.accessioned
2020-02-03T09:55:19Z
dc.date.available
2020-02-03T03:46:40Z
dc.date.available
2020-02-03T09:55:19Z
dc.date.issued
2020
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/s41467-019-14179-x
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/396587
dc.identifier.doi
10.3929/ethz-b-000396587
dc.description.abstract
Characterizing folding and complex formation of biomolecules provides a view into their thermodynamics, kinetics and folding pathways. Deciphering kinetic intermediates is particularly important because they can often be targeted by drugs. The key advantage of native mass spectrometry over conventional methods that monitor a single observable is its ability to identify and quantify coexisting species. Here, we show the design of a temperature-jump electrospray source for mass spectrometry that allows one to perform fast kinetics experiments (0.16–32 s) at different temperatures (10–90 °C). The setup allows recording of both folding and unfolding kinetics by using temperature jumps from high to low, and low to high, temperatures. Six biological systems, ranging from peptides to proteins to DNA complexes, exemplify the use of this device. Using temperature-dependent experiments, the folding and unfolding of a DNA triplex are studied, providing detailed information on its thermodynamics and kinetics.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Studying biomolecular folding and binding using temperature-jump mass spectrometry
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2020-01-28
ethz.journal.title
Nature Communications
ethz.journal.volume
11
en_US
ethz.journal.issue
1
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
566
en_US
ethz.size
12 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
Soft ionization mass spectrometry for studying noncovalent interactions
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
London
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.::02514 - Laboratorium für Organische Chemie / Laboratory of Organic Chemistry::03430 - Zenobi, Renato / Zenobi, Renato
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.::02514 - Laboratorium für Organische Chemie / Laboratory of Organic Chemistry::03430 - Zenobi, Renato / Zenobi, Renato
ethz.grant.agreementno
178765
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
Projektförderung in Mathematik, Natur- und Ingenieurwissenschaften (Abteilung II)
ethz.relation.isSupplementedBy
10.3929/ethz-b-000353280
ethz.relation.isSupplementedBy
10.3929/ethz-b-000385801
ethz.date.deposited
2020-02-03T03:46:44Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2020-02-03T09:55:33Z
ethz.rosetta.lastUpdated
2020-02-15T23:58:35Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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