Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

We describe a general mass spectrometry approach to determine subunit stoichiometry and lipid binding in intact membrane protein complexes. By exploring conditions for preserving interactions during transmission into the gas phase and for optimally stripping away detergent, by subjecting the complex to multiple collisions, we released the intact complex largely devoid of detergent. This enabled us to characterize both subunit stoichiometry and lipid binding in 4 membrane protein complexes.

Original publication

DOI

10.1038/nmeth.1347

Type

Journal article

Journal

Nat Methods

Publication Date

08/2009

Volume

6

Pages

585 - 587

Keywords

Membrane Transport Proteins, Multiprotein Complexes, Protein Interaction Mapping, Protein Subunits, Proteomics, Spectrometry, Mass, Electrospray Ionization