Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics

Detergents are often used to investigate the structure and dynamics of membrane proteins. Whereas the structural integrity seems to be preserved in detergents for many membrane proteins, their functional activity is frequently compromised, but can be restored in a lipid environment. Herein we show w...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2017-01, Vol.56 (1), p.380-383
Main Authors: Frey, Lukas, Lakomek, Nils‐Alexander, Riek, Roland, Bibow, Stefan
Format: Article
Language:English
Subjects:
Bacterial Outer Membrane Proteins - chemistry
Communication
Communications
Detergents
Dynamic structural analysis
Escherichia coli Proteins - chemistry
Hydrolases - chemistry
Lipids
Membrane proteins
Micelles
Molecular Dynamics Simulation
Nanostructures - chemistry
NMR spectroscopy
OmpX
Phosphorylcholine - analogs & derivatives
Phosphorylcholine - chemistry
protein dynamics
Protein structure
Proteins
relaxation
Structural integrity
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Summary:Detergents are often used to investigate the structure and dynamics of membrane proteins. Whereas the structural integrity seems to be preserved in detergents for many membrane proteins, their functional activity is frequently compromised, but can be restored in a lipid environment. Herein we show with per‐residue resolution that while OmpX forms a stable β‐barrel in DPC detergent micelles, DHPC/DMPC bicelles, and DMPC nanodiscs, the pico‐ to nanosecond and micro‐ to millisecond motions differ substantially between the detergent and lipid environment. In particular for the β‐strands, there is pronounced dynamic variability in the lipid environment, which appears to be suppressed in micelles. This unexpected complex and membrane‐mimetic‐dependent dynamic behavior indicates that the frequent loss of membrane protein activity in detergents might be related to reduced internal dynamics and that membrane protein activity correlates with lipid flexibility. The outer membrane protein X (OmpX) forms a stable β‐barrel in DPC detergent micelles, DHPC/DMPC bicelles, and DMPC nanodiscs but its dynamics on the pico‐ to nanosecond and micro‐ to millisecond timescale differ significantly for the detergent and lipid environments. This dynamic behavior could explain the loss of membrane protein activity frequently observed in detergents.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201608246