Studying biomolecular folding and binding using temperature-jump mass spectrometry

Studying biomolecular folding and binding using temperature-jump mass spectrometry

Native mass spectrometry allows monitoring the folding and interactions of multiple coexisting species but its temporal resolution is traditionally limited. Here, the authors develop a temperature-jump electrospray source for mass spectrometry that enables fast kinetics experiments at different temp...

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Bibliographic Details
Main Authors: Adrien Marchand, Martin F. Czar, Elija N. Eggel, Jérôme Kaeslin, Renato Zenobi
Format: Article
Language:English
Published: Nature Publishing Group 2020-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-14179-x
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spelling doaj-2bc797ec27904e3bb266623df48cef4e2021-05-11T08:57:49ZengNature Publishing GroupNature Communications2041-17232020-01-0111111210.1038/s41467-019-14179-xStudying biomolecular folding and binding using temperature-jump mass spectrometryAdrien Marchand0Martin F. Czar1Elija N. Eggel2Jérôme Kaeslin3Renato Zenobi4Department of Chemistry and Applied Biosciences, ETH ZurichDepartment of Chemistry and Applied Biosciences, ETH ZurichDepartment of Chemistry and Applied Biosciences, ETH ZurichDepartment of Chemistry and Applied Biosciences, ETH ZurichDepartment of Chemistry and Applied Biosciences, ETH ZurichNative mass spectrometry allows monitoring the folding and interactions of multiple coexisting species but its temporal resolution is traditionally limited. Here, the authors develop a temperature-jump electrospray source for mass spectrometry that enables fast kinetics experiments at different temperatures.https://doi.org/10.1038/s41467-019-14179-x
collection DOAJ
language English
format Article
sources DOAJ
author Adrien Marchand
Martin F. Czar
Elija N. Eggel
Jérôme Kaeslin
Renato Zenobi
spellingShingle Adrien Marchand
Martin F. Czar
Elija N. Eggel
Jérôme Kaeslin
Renato Zenobi
Studying biomolecular folding and binding using temperature-jump mass spectrometry
Nature Communications
author_facet Adrien Marchand
Martin F. Czar
Elija N. Eggel
Jérôme Kaeslin
Renato Zenobi
author_sort Adrien Marchand
title Studying biomolecular folding and binding using temperature-jump mass spectrometry
title_short Studying biomolecular folding and binding using temperature-jump mass spectrometry
title_full Studying biomolecular folding and binding using temperature-jump mass spectrometry
title_fullStr Studying biomolecular folding and binding using temperature-jump mass spectrometry
title_full_unstemmed Studying biomolecular folding and binding using temperature-jump mass spectrometry
title_sort studying biomolecular folding and binding using temperature-jump mass spectrometry
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-01-01
description Native mass spectrometry allows monitoring the folding and interactions of multiple coexisting species but its temporal resolution is traditionally limited. Here, the authors develop a temperature-jump electrospray source for mass spectrometry that enables fast kinetics experiments at different temperatures.
url https://doi.org/10.1038/s41467-019-14179-x
work_keys_str_mv AT adrienmarchand studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry
AT martinfczar studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry
AT elijaneggel studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry
AT jeromekaeslin studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry
AT renatozenobi studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry
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