What’s the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry
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Final Accepted Manuscript
Affiliation
Department of Chemistry and Biochemistry, University of ArizonaBio5 Institute, University of Arizona
Issue Date
2023-07-22Keywords
LipidsMass defect analysis
Membrane proteins
Nanodiscs
Native mass spectrometry
Oligomerization
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Elsevier BVCitation
Townsend, J. A., & Marty, M. T. (2023). What’s the defect? Using mass defects to study oligomerization of membrane proteins and peptides in nanodiscs with native mass spectrometry. Methods.Journal
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© 2023 Elsevier Inc. All rights reserved.Collection Information
This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.Abstract
Many membrane proteins form functional complexes that are either homo- or hetero-oligomeric. However, it is challenging to characterize membrane protein oligomerization in intact lipid bilayers, especially for polydisperse mixtures. Native mass spectrometry of membrane proteins and peptides inserted in lipid nanodiscs provides a unique method to study the oligomeric state distribution and lipid preferences of oligomeric assemblies. To interpret these complex spectra, we developed novel data analysis methods using macromolecular mass defect analysis. Here, we provide an overview of how mass defect analysis can be used to study oligomerization in nanodiscs, discuss potential limitations in interpretation, and explore strategies to resolve these ambiguities. Finally, we review recent work applying this technique to studying formation of antimicrobial peptide, amyloid protein, and viroporin complexes with lipid membranes.Note
12 month embargo; first published 22 July 2023ISSN
1046-2023Version
Final accepted manuscriptae974a485f413a2113503eed53cd6c53
10.1016/j.ymeth.2023.07.004