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Whitelegge J. Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome. Proteomes. 2020;8(1)doi: 10.3390/proteomes8010005.
Whitelegge, J. (2020). Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome. Proteomes, 8(1), . https://doi.org/10.3390/proteomes8010005
Whitelegge, Julian. "Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome." Proteomes vol. 8,1 (2020). doi: https://doi.org/10.3390/proteomes8010005
Whitelegge J. Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome. Proteomes. 2020 Mar 10;8(1). doi: 10.3390/proteomes8010005. PMID: 32164246; PMCID: PMC7151669.
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Proteomes. 2020 Mar 10;8(1). doi: 10.3390/proteomes8010005.

Targeting a Subset of the Membrane Proteome for Top-Down Mass Spectrometry: Introducing the Proteolipidome.

Proteomes

Julian Whitelegge

Affiliations

  1. The Pasarow Mass Spectrometry Laboratory, Jane and Terry Semel Institute of Neuroscience and Human Behavior, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, CA 90095 USA.

PMID: 32164246 PMCID: PMC7151669 DOI: 10.3390/proteomes8010005

Abstract

A subsection of integral membrane proteins partition into chloroform during a chloroform/methanol/water extraction primarily designed to extract lipids. Traditionally, these proteins were called proteolipids due to their lipid-like properties; the c-subunit of the ATP synthase integral FO component is the best known due to its abundance. In this manuscript, we investigate purification of proteolipid proteins away from lipids for high-resolution mass spectrometry. Size-exclusion chromatography on silica beads using a chloroform/methanol/aqueous formic acid (4/4/1;

Keywords: CAD; FTICR; aiECD; high-resolution mass spectrometry; proteoform

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