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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Autores principales:	Adrien Marchand, Martin F. Czar, Elija N. Eggel, Jérôme Kaeslin, Renato Zenobi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/2bc797ec27904e3bb266623df48cef4e
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id	oai:doaj.org-article:2bc797ec27904e3bb266623df48cef4e
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spelling	oai:doaj.org-article:2bc797ec27904e3bb266623df48cef4e2021-12-02T15:39:26ZStudying biomolecular folding and binding using temperature-jump mass spectrometry10.1038/s41467-019-14179-x2041-1723https://doaj.org/article/2bc797ec27904e3bb266623df48cef4e2020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-14179-xhttps://doaj.org/toc/2041-1723Native 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.Adrien MarchandMartin F. CzarElija N. EggelJérôme KaeslinRenato ZenobiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Adrien Marchand Martin F. Czar Elija N. Eggel Jérôme Kaeslin Renato Zenobi Studying biomolecular folding and binding using temperature-jump mass spectrometry
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.
format	article
author	Adrien Marchand Martin F. Czar Elija N. Eggel Jérôme Kaeslin Renato Zenobi
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 Portfolio
publishDate	2020
url	https://doaj.org/article/2bc797ec27904e3bb266623df48cef4e
work_keys_str_mv	AT adrienmarchand studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry AT martinfczar studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry AT elijaneggel studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry AT jeromekaeslin studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry AT renatozenobi studyingbiomolecularfoldingandbindingusingtemperaturejumpmassspectrometry
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Studying biomolecular folding and binding using temperature-jump mass spectrometry

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