Hammerschmid, D, van Dyck, JF, Sobott, F orcid.org/0000-0001-9029-1865 et al. (1 more author) (2021) Interrogating Membrane Protein Structure and Lipid Interactions by native mass spectrometry. In: Postis, VLG and Goldman, A, (eds.) Biophysics of Membrane Proteins: Methods and Protocols. Methods in Molecular Biology, 2168 . Springer US , New York, USA , pp. 233-261. ISBN 978-1-0716-0723-7
Abstract
Native mass spectrometry and native ion mobility mass spectrometry are now established techniques in structural biology, with recent work developing these methods for the study of integral membrane proteins reconstituted in both lipid bilayer and detergent environments. Here we show how native mass spectrometry can be used to interrogate integral membrane proteins, providing insights into conformation, oligomerization, subunit composition/stoichiometry, and interactions with detergents/lipids/drugs. Furthermore, we discuss the sample requirements and experimental considerations unique to integral membrane protein native mass spectrometry research.
Metadata
Item Type: | Book Section |
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Authors/Creators: |
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Editors: |
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Copyright, Publisher and Additional Information: | © Springer Science+Business Media, LLC, part of Springer Nature 2020. This is an author produced version of a book chapter published in Biophysics of Membrane Proteins: Methods and Protocols. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Native mass spectrometry; Ion mobility; Membrane proteins; Detergent micelles; Lipids |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biomolecular Mass Spectroscopy (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 Mar 2021 11:26 |
Last Modified: | 14 Feb 2023 01:13 |
Status: | Published |
Publisher: | Springer US |
Series Name: | Methods in Molecular Biology |
Identification Number: | 10.1007/978-1-0716-0724-4_11 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:172461 |