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Interrogating Membrane Protein Conformational Dynamics within Native Lipid Compositions
Author(s) -
Reading Eamonn,
Hall Zoe,
Martens Chloe,
Haghighi Tabasom,
Findlay Heather,
Ahdash Zainab,
Politis Argyris,
Booth Paula J.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201709657
Subject(s) - chemistry , lipid bilayer , protein dynamics , biophysics , membrane protein , membrane , dynamics (music) , peripheral membrane protein , molecular dynamics , native state , protein structure , biochemistry , biology , integral membrane protein , physics , computational chemistry , acoustics
The interplay between membrane proteins and the lipids of the membrane is important for cellular function, however, tools enabling the interrogation of protein dynamics within native lipid environments are scarce and often invasive. We show that the styrene–maleic acid 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.