ArticleAnalytical and bioanalytical chemistry2012
Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs.
Article in Analytical and bioanalytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020Article
- Time-of-flight secondary ion mass spectrometry three-dimensional imaging of surface modifications in poly(caprolactone) scaffold pores.Journal of biomedical materials research. Part A · 2019Article
- Regulation of Membrane Calcium Transport Proteins by the Surrounding Lipid Environment.Biomolecules · 2019Review
- Mechanism of metal ion-induced activation of a two-component sensor kinase.The Biochemical journal · 2019Article
- Nanodiscs: A Controlled Bilayer Surface for the Study of Membrane Proteins.Annual review of biophysics · 2018Article
- Review
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Combining Mass Spectrometry and X-Ray Crystallography for Analyzing Native-Like Membrane Protein Lipid Complexes.Frontiers in physiology · 2017Article
- Functional studies of N-terminally modified CYP2J2 epoxygenase in model lipid bilayers.Protein science : a publication of the Protein Society · 2013Article
- Lipid nanotechnology.International journal of molecular sciences · 2013Article
- Nanodiscs as a new tool to examine lipid-protein interactions.Methods in molecular biology (Clifton, N.J.) · 2013Review
- Amphipathic polymers enable the study of functional membrane proteins in the gas phase.Analytical chemistry · 2012Article
- Native mass spectrometry characterization of intact nanodisc lipoprotein complexes.Analytical chemistry · 2012Article
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Authors and funding
3 authors.
Funding
Abstract
Nanodiscs have become a leading technology to solubilize membrane proteins for biophysical, enzymatic, and structural investigations. Nanodiscs are nanoscale, discoidal lipid bilayers surrounded by an amphipathic membrane scaffold protein (MSP) belt. A variety of analytical tools has been applied to membrane proteins in nanodiscs, including several recent mass spectrometry studies. Mass spectrometry of full-length proteins is an important technique for analyzing protein modifications, for structural studies, and for identification of proteins present in binding assays. However, traditional matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF) mass spectrometry methods for analyzing full-length membrane proteins solubilized in nanodiscs are limited by strong signal from the MSP belt and weak signal from the membrane protein inside the nanodisc. Herein, we show that an optimized ultra-thin layer MALDI sample preparation technique dramatically enhances the membrane protein signal and nearly completely eliminates the MSP signal. First-shot MALDI and MALDI imaging are used to characterize the spots formed by the ultra-thin layer method. Furthermore, the membrane protein enhancement and MSP suppression are shown to be independent of the type of membrane protein and are applicable to mixtures of membrane proteins in nanodiscs.
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