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dc.contributor.author
Sturzenegger, Flurin
dc.contributor.author
Zosel, Franziska
dc.contributor.author
Holmstrom, Erik D.
dc.contributor.author
Buholzer, Karin J.
dc.contributor.author
Makarov, Dmitrii E.
dc.contributor.author
Nettels, Daniel
dc.contributor.author
Schuler, Benjamin
dc.date.accessioned
2019-01-23T14:11:20Z
dc.date.available
2019-01-23T08:28:20Z
dc.date.available
2019-01-23T14:11:20Z
dc.date.issued
2018-11-09
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/s41467-018-07043-x
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/318763
dc.identifier.doi
10.3929/ethz-b-000318763
dc.description.abstract
The association of biomolecules is the elementary event of communication in biology. Most mechanistic information of how the interactions between binding partners form or break is, however, hidden in the transition paths, the very short parts of the molecular trajectories from the encounter of the two molecules to the formation of a stable complex. Here we use single-molecule spectroscopy to measure the transition path times for the association of two intrinsically disordered proteins that form a folded dimer upon binding. The results reveal the formation of a metastable encounter complex that is electrostatically favored and transits to the final bound state within tens of microseconds. Such measurements thus open a new window into the microscopic events governing biomolecular interactions.
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.subject
Biophysics
en_US
dc.subject
Intrinsically disordered proteins
en_US
dc.subject
Kinetics
en_US
dc.subject
Molecular biophysics
en_US
dc.subject
Molecular conformation
en_US
dc.title
Transition path times of coupled folding and binding reveal the formation of an encounter complex
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
Nature Communications
ethz.journal.volume
9
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
4708
en_US
ethz.size
11 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00003 - Schulleitung und Dienste::00022 - Bereich VP Forschung / Domain VP Research::02207 - Functional Genomics Center Zurich / Functional Genomics Center Zurich
en_US
ethz.date.deposited
2019-01-23T08:28:28Z
ethz.source
FORM
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2019-01-23T14:11:34Z
ethz.rosetta.lastUpdated
2021-02-15T03:25:09Z
ethz.rosetta.versionExported
true
ethz.COinS
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