Studying biomolecular folding and binding using temperature-jump mass spectrometry

Open access
Date
2020Type
- Journal Article
Citations
Cited 22 times in
Web of Science
Cited 20 times in
Scopus
ETH Bibliography
yes
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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. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000396587Publication status
publishedExternal links
Journal / series
Nature CommunicationsVolume
Pages / Article No.
Publisher
Nature Publishing GroupOrganisational unit
03430 - Zenobi, Renato / Zenobi, Renato
Funding
178765 - Soft ionization mass spectrometry for studying noncovalent interactions (SNF)
Related publications and datasets
Is supplemented by: https://doi.org/10.3929/ethz-b-000353280
Is supplemented by: https://doi.org/10.3929/ethz-b-000385801
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Show all metadata
Citations
Cited 22 times in
Web of Science
Cited 20 times in
Scopus
ETH Bibliography
yes
Altmetrics