Structural Characterization of an Integral Membrane Protein in Its Natural Lipid Environment by Oxidative Methionine Labeling and Mass Spectrometry

2009 ◽  
Vol 81 (1) ◽  
pp. 28-35 ◽  
Author(s):  
Yan Pan ◽  
Bradley B. Stocks ◽  
Leonid Brown ◽  
Lars Konermann
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Structural Characterization ◽  
Integral Membrane Protein ◽  
Lipid Environment ◽  
Natural Lipid

scholarly journals Analyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biology

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Erik Henrich ◽  
Oliver Peetz ◽  
Christopher Hein ◽  
Aisha Laguerre ◽  
Beate Hoffmann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Synthetic Biology ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Molecular Mechanisms ◽  
Protein Oligomerization ◽  
Protein Assemblies ◽  
Oligomeric State ◽  
Lipid Environment

Membrane proteins frequently assemble into higher order homo- or hetero-oligomers within their natural lipid environment. This complex formation can modulate their folding, activity as well as substrate selectivity. Non-disruptive methods avoiding critical steps, such as membrane disintegration, transfer into artificial environments or chemical modifications are therefore essential to analyze molecular mechanisms of native membrane protein assemblies. The combination of cell-free synthetic biology, nanodisc-technology and non-covalent mass spectrometry provides excellent synergies for the analysis of membrane protein oligomerization within defined membranes. We exemplify our strategy by oligomeric state characterization of various membrane proteins including ion channels, transporters and membrane-integrated enzymes assembling up to hexameric complexes. We further indicate a lipid-dependent dimer formation of MraY translocase correlating with the enzymatic activity. The detergent-free synthesis of membrane protein/nanodisc samples and the analysis by LILBID mass spectrometry provide a versatile platform for the analysis of membrane proteins in a native environment.

Structural Characterization of Bacillus subtilis Membrane Protein Bmr: An In Silico Approach

2015 ◽  
Vol 10 (3) ◽  
pp. 226-236
Author(s):  
Amit Nargotra ◽  
Rukmankesh ◽  
Shakir Ali ◽  
Surrinder Koul
Keyword(s):  
Bacillus Subtilis ◽  
Membrane Protein ◽  
Structural Characterization ◽  
In Silico

Structural characterization of chelator-terminated dendrimers and their synthetic intermediates by mass spectrometry

2005 ◽  
Vol 40 (9) ◽  
pp. 1203-1214 ◽  
Author(s):  
Ursula E. Ch. Berndt ◽  
Tao Zhou ◽  
Robert C. Hider ◽  
Zu D. Liu ◽  
Hendrik Neubert
Keyword(s):  
Mass Spectrometry ◽  
Structural Characterization ◽  
Synthetic Intermediates
Sign in / Sign up

Export Citation Format

Share Document