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High-resolution mass spectrometry of small molecules bound to membrane proteins.

ABSTRACT: Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry-based method for analyzing intact membrane protein-ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length.

SUBMITTER: Gault J

PROVIDER: S-EPMC4856209 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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High-resolution mass spectrometry of small molecules bound to membrane proteins.

Gault Joseph J Donlan Joseph A C JA Liko Idlir I Hopper Jonathan T S JT Gupta Kallol K Housden Nicholas G NG Struwe Weston B WB Marty Michael T MT Mize Todd T Bechara Cherine C Zhu Ya Y Wu Beili B Kleanthous Colin C Belov Mikhail M Damoc Eugen E Makarov Alexander A Robinson Carol V CV

Nature methods 20160222 4

Small molecules are known to stabilize membrane proteins and to modulate their function and oligomeric state, but such interactions are often hard to precisely define. Here we develop and apply a high-resolution, Orbitrap mass spectrometry-based method for analyzing intact membrane protein-ligand complexes. Using this platform, we resolve the complexity of multiple binding events, quantify small molecule binding and reveal selectivity for endogenous lipids that differ only in acyl chain length. ...[more]

PMID: 26901650

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