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- W3009896878 abstract "Native mass spectrometry is an emerging technique in biology that gives the possibility to study noncovalently bound complexes with high sensitivity and accuracy. It thus allows the characterization of macromolecular assemblies, assessing their mass and stoichiometries and mapping the interacting surfaces. In this review, we discuss the application of native mass spectrometry to dynamic molecular machines based on multiple weak interactions. In the study of these machines, it is crucial to understand which and under which conditions various complexes form at any time point. We focus on the specific example of the iron-sulfur cluster biogenesis machine because this is an archetype of a dynamic machine that requires very specific and demanding experimental conditions, such as anaerobicity and the need of retaining the fold of marginally folded proteins. We describe the advantages, challenges and current limitations of the technique by providing examples from our own experience and suggesting possible future solutions." @default.
- W3009896878 created "2020-03-13" @default.
- W3009896878 creator A5019979618 @default.
- W3009896878 creator A5039746487 @default.
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- W3009896878 date "2020-03-25" @default.
- W3009896878 modified "2023-10-18" @default.
- W3009896878 title "A Guide to Native Mass Spectrometry to determine complex interactomes of molecular machines" @default.
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- W3009896878 doi "https://doi.org/10.1111/febs.15281" @default.
- W3009896878 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32142206" @default.
- W3009896878 hasPublicationYear "2020" @default.
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