Mass spectrometry of full-length integral membrane proteins to define functionally relevant structural features

Methods ◽  
2008 ◽  
Vol 46 (2) ◽  
pp. 54-61 ◽  
Author(s):  
Guillaume Gabant ◽  
Martine Cadene
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Structural Features ◽  
Full Length ◽  
Integral Membrane Proteins

Top-down mass spectrometry of integral membrane proteins

2006 ◽  
Vol 3 (6) ◽  
pp. 585-596 ◽  
Author(s):  
Julian Whitelegge ◽  
Frederic Halgand ◽  
Puneet Souda ◽  
Vlad Zabrouskov
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Integral Membrane Proteins ◽  
Top Down ◽  
Top Down Mass Spectrometry

scholarly journals Scratching the surface: native mass spectrometry of peripheral membrane protein complexes

2020 ◽  
Vol 48 (2) ◽  
pp. 547-558 ◽  
Author(s):  
Cagla Sahin ◽  
Deseree J. Reid ◽  
Michael T. Marty ◽  
Michael Landreh
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Vesicles ◽  
Native Mass Spectrometry ◽  
Integral Membrane Proteins ◽  
Structural Basis ◽  
Lipid Interactions ◽  
Native Ms ◽  
Peripheral Membrane Protein

A growing number of integral membrane proteins have been shown to tune their activity by selectively interacting with specific lipids. The ability to regulate biological functions via lipid interactions extends to the diverse group of proteins that associate only peripherally with the lipid bilayer. However, the structural basis of these interactions remains challenging to study due to their transient and promiscuous nature. Recently, native mass spectrometry has come into focus as a new tool to investigate lipid interactions in membrane proteins. Here, we outline how the native MS strategies developed for integral membrane proteins can be applied to generate insights into the structure and function of peripheral membrane proteins. Specifically, native MS studies of proteins in complex with detergent-solubilized lipids, bound to lipid nanodiscs, and released from native-like lipid vesicles all shed new light on the role of lipid interactions. The unique ability of native MS to capture and interrogate protein–protein, protein–ligand, and protein–lipid interactions opens exciting new avenues for the study of peripheral membrane protein biology.

Strategies for shotgun identification of integral membrane proteins by tandem mass spectrometry

PROTEOMICS ◽  
2008 ◽  
Vol 8 (19) ◽  
pp. 3947-3955 ◽  
Author(s):  
Bingwen Lu ◽  
Daniel B. McClatchy ◽  
Jin Young Kim ◽  
John R. Yates
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Tandem Mass Spectrometry ◽  
Integral Membrane Proteins ◽  
Tandem Mass
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