Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics
OPEN ACCESS
Loading...
Author / Producer
Date
2017-01-02
Publication Type
Journal Article
ETH Bibliography
yes
Citations
Altmetric
OPEN ACCESS
Data
Abstract
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.
Permanent link
Publication status
published
External links
Editor
Book title
Journal / series
Volume
56 (1)
Pages / Article No.
380 - 383
Publisher
Wiley-VCH
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
membrane proteins; NMR spectroscopy; OmpX; protein dynamics; relaxation
Organisational unit
03782 - Riek, Roland / Riek, Roland
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
Notes
Published online 24 November 2016.
Funding
154461 - The Time- and Spatially Resolved Aggregation of a-Synuclein and its Relationship to Cell-Cell Transmissibility (SNF)