ArticleAnalytical chemistry2012
Amphipathic polymers enable the study of functional membrane proteins in the gas phase.
Article in Analytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Structural mass spectrometry approaches to understand multidrug efflux systems.Essays in biochemistry · 2023Review
- Native Mass Spectrometry: Recent Progress and Remaining Challenges.Annual review of biophysics · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Approaches to Heterogeneity in Native Mass Spectrometry.Chemical reviews · 2022Review
- Native Mass Spectrometry and Surface Induced Dissociation Provide Insight into the Post-Translational Modifications of Tetrameric AQP0 Isolated from Bovine Eye Lens.Analytical chemistry · 2022Article
- Styrene maleic-acid lipid particles (SMALPs) into detergent or amphipols: An exchange protocol for membrane protein characterisation.Biochimica et biophysica acta. Biomembranes · 2020Article
- Scratching the surface: native mass spectrometry of peripheral membrane protein complexes.Biochemical Society transactions · 2020Review
- Expanding the Types of Lipids Amenable to Native Mass Spectrometry of Lipoprotein Complexes.Journal of the American Society for Mass Spectrometry · 2019Article
- Insights into the Basal Activity and Activation Mechanism of the β1 Adrenergic Receptor Using Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019Article
- Salvaging the Thermodynamic Destabilization of Interface Histidine in Transmembrane β-Barrels.Biochemistry · 2018Article
- Stabilization of a Membrane-Associated Amyloid-β Oligomer for Its Validation in Alzheimer's Disease.Frontiers in molecular biosciences · 2018Article
- Surface induced dissociation as a tool to study membrane protein complexes.Chemical communications (Cambridge, England) · 2017Article
- FPOP-LC-MS/MS Suggests Differences in Interaction Sites of Amphipols and Detergents with Outer Membrane Proteins.Journal of the American Society for Mass Spectrometry · 2017Article
- Native Mass Spectrometry: What is in the Name?Journal of the American Society for Mass Spectrometry · 2017Article
- Native MS Analysis of Bacteriorhodopsin and an Empty Nanodisc by Orthogonal Acceleration Time-of-Flight, Orbitrap and Ion Cyclotron Resonance.Analytical chemistry · 2016Article
- Interfacing Membrane Mimetics with Mass Spectrometry.Accounts of chemical research · 2016Article
- A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis.Biochemical Society transactions · 2016Review
- Systematic analysis of the use of amphipathic polymers for studies of outer membrane proteins using mass spectrometry.International journal of mass spectrometry · 2015Article
- Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Analytical chemistry · 2015Article
- Synthesis, characterization and applications of a perdeuterated amphipol.The Journal of membrane biology · 2014Article
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4 authors.
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Abstract
Membrane proteins are notoriously challenging to analyze using mass spectrometry (MS) because of their insolubility in aqueous solution. Current MS methods for studying intact membrane proteins involve solubilization in detergent. However, detergents can destabilize proteins, leading to protein unfolding and aggregation, or resulting in inactive entities. Amphipathic polymers, termed amphipols, can be used as a substitute for detergents and have been shown to enhance the stability of membrane proteins. Here, we show the utility of amphipols for investigating the structural and functional properties of membrane proteins using electrospray ionization mass spectrometry (ESI-MS). The functional properties of two bacterial outer-membrane β-barrel proteins, OmpT and PagP, in complex with the amphipol A8-35 are demonstrated, and their structural integrities are confirmed in the gas phase using ESI-MS coupled with ion mobility spectrometry (IMS). The data illustrate the power of ESI-IMS-MS in separating distinct populations of amphipathic polymers from the amphipol-membrane complex while maintaining a conformationally "nativelike" membrane protein structure in the gas phase. Together, the data indicate the potential importance and utility of amphipols for the analysis of membrane proteins using MS.
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Registered trials
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