Generation of Charge-Reduced Ions of Membrane Protein Complexes for Native Ion Mobility Mass Spectrometry Studies. Academic Article

abstract

• Recent advances in native mass spectrometry (MS) have enabled the elucidation of how small molecule binding to membrane proteins modulates their structure and function. The protein-stabilizing osmolyte, trimethylamine oxide (TMAO), exhibits attractive properties for native MS studies. Here, we report significant charge reduction, nearly threefold, for three membrane protein complexes in the presence of this osmolyte without compromising mass spectral resolution. TMAO improves the ability to resolve individual lipid-binding events to the ammonia channel (AmtB) by over 200% compared to typical native conditions. The generation of ions with compact structure and access to a larger number of lipid-binding events through the incorporation of TMAO increases the utility of IM-MS for structural biology studies. Graphical Abstract.

authors

• Laganowsky, Arthur

published proceedings

• J Am Soc Mass Spectrom

altmetric score

• 1.75

author list (cited authors)

• Patrick, J. W., & Laganowsky, A.

citation count

• 11

complete list of authors

• Patrick, John W||Laganowsky, Arthur

publication date

• May 2019

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Society for Mass Spectrometry  Journal

keywords

• Aquaporins
• Bacterial Proteins
• Cation Transport Proteins
• Escherichia Coli
• Escherichia Coli Proteins
• Excipients
• Ion Channels
• Ion Mobility
• Ion Mobility Spectrometry
• Ions
• Lipid
• Membrane Protein
• Methylamines
• Mycobacterium Tuberculosis
• Native Mass Spectrometry
• Protein Conformation

PubMed Central ID

• 30887461

Digital Object Identifier (DOI)

• 10.1007/s13361-019-02187-6

start page

• 886

end page

• 892

volume

• 30

issue

• 5

URL

• http://dx.doi.org/10.1007/s13361-019-02187-6