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Interrogating membrane protein conformational dynamics within native lipid compositions

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)15654*15657
JournalANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume56
Issue number49
Early online date8 Nov 2017
DOIs
Accepted/In press19 Oct 2017
E-pub ahead of print8 Nov 2017

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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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