Interrogating membrane protein conformational dynamics within native lipid compositions

Eamonn Reading; Zoe Hall; Chloe Martens; Tabasom Haghighi; Heather Findlay; Zainab Ahdash; Argyris Politis; Paula J Booth

doi:10.1002/anie.201709657

Interrogating membrane protein conformational dynamics within native lipid compositions

Eamonn Reading, Zoe Hall, Chloe Martens, Tabasom Haghighi, Heather Findlay, Zainab Ahdash, Argyris Politis, Paula J Booth

Chemistry

Kings College London, Chemistry, Britannia House, 7 Trinity Street, SE1 1DB, London, UNITED KINGDOM.

Research output: Contribution to journal › Article › peer-review

76 Citations (Scopus)

279 Downloads (Pure)

Abstract

Membrane protein-lipid interplay is important for cellular function, however, tools enabling the interrogation of protein dynamics within native lipid environments are scarce and often invasive. We establish that the styrene-maleic acid anhydride lipid particle (SMALP) technology can be coupled with hydrogen-deuterium exchange mass spectrometry (HDX-MS) to investigate membrane protein conformational dynamics within native lipid bilayers. We demonstrate changes in accessibility and dynamics of the rhomboid protease, GlpG, captured within three different native lipid compositions, and identify protein regions sensitive to changes in the native lipid environment. Our results illuminate the value of this approach for distinguishing the putative role(s) of the native lipid composition in modulating membrane protein conformational dynamics.

Original language	English
Pages (from-to)	15654*15657
Journal	ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume	56
Issue number	49
Early online date	8 Nov 2017
DOIs	https://doi.org/10.1002/anie.201709657
Publication status	E-pub ahead of print - 8 Nov 2017

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10.1002/anie.201709657

Interrogating membrane protein conformational_READING_Publishedonline8November2017_GREEN AAMAccepted author manuscript, 6.54 MB

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title = "Interrogating membrane protein conformational dynamics within native lipid compositions",

abstract = "Membrane protein-lipid interplay is important for cellular function, however, tools enabling the interrogation of protein dynamics within native lipid environments are scarce and often invasive. We establish that the styrene-maleic acid anhydride lipid particle (SMALP) technology can be coupled with hydrogen-deuterium exchange mass spectrometry (HDX-MS) to investigate membrane protein conformational dynamics within native lipid bilayers. We demonstrate changes in accessibility and dynamics of the rhomboid protease, GlpG, captured within three different native lipid compositions, and identify protein regions sensitive to changes in the native lipid environment. Our results illuminate the value of this approach for distinguishing the putative role(s) of the native lipid composition in modulating membrane protein conformational dynamics.",

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AU - Martens, Chloe

AU - Haghighi, Tabasom

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AU - Ahdash, Zainab

AU - Politis, Argyris

AU - Booth, Paula J

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Interrogating membrane protein conformational dynamics within native lipid compositions

Abstract

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