scholarly journals Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs

2018 ◽  
Vol 54 (97) ◽  
pp. 13702-13705 ◽  
Author(s):  
Nils Hellwig ◽  
Oliver Peetz ◽  
Zainab Ahdash ◽  
Igor Tascón ◽  
Paula J. Booth ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayer ◽  
Maleic Acid ◽  
Protein Complexes ◽  
Native Mass Spectrometry ◽  
Direct Extraction ◽  
Membrane Protein Complexes

Other than more widely used methods, the use of styrene maleic acid copolymers allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding.

scholarly journals Mass spectrometry of membrane protein complexes

2019 ◽  
Vol 400 (7) ◽  
pp. 813-829 ◽  
Author(s):  
Julian Bender ◽  
Carla Schmidt
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Three Dimensional ◽  
Membrane Protein Complexes ◽  
Hydrophobic Nature ◽  
Alternative Approaches ◽  
Lipid Environment ◽  
And Function

Abstract Membrane proteins are key players in the cell. Due to their hydrophobic nature they require solubilising agents such as detergents or membrane mimetics during purification and, consequently, are challenging targets in structural biology. In addition, their natural lipid environment is crucial for their structure and function further hampering their analysis. Alternative approaches are therefore required when the analysis by conventional techniques proves difficult. In this review, we highlight the broad application of mass spectrometry (MS) for the characterisation of membrane proteins and their interactions with lipids. We show that MS unambiguously identifies the protein and lipid components of membrane protein complexes, unravels their three-dimensional arrangements and further provides clues of protein-lipid interactions.

Three-dimensional crystallization of membrane proteins

1988 ◽  
Vol 21 (4) ◽  
pp. 429-477 ◽  
Author(s):  
W. Kühlbrandt
Keyword(s):  
High Resolution ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Three Dimensional ◽  
Biological Macromolecules ◽  
X Ray ◽  
X Ray Crystallography ◽  
Membrane Protein Complexes ◽  
Essential Prerequisite

As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.

scholarly journals Mass spectrometry of intact membrane protein complexes

2013 ◽  
Vol 8 (4) ◽  
pp. 639-651 ◽  
Author(s):  
Arthur Laganowsky ◽  
Eamonn Reading ◽  
Jonathan T S Hopper ◽  
Carol V Robinson
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Intact Membrane ◽  
Membrane Protein Complexes

scholarly journals Controlling release, unfolding and dissociation of membrane protein complexes in the gas phase through collisional cooling

2015 ◽  
Vol 51 (85) ◽  
pp. 15582-15584 ◽  
Author(s):  
Michael Landreh ◽  
Idlir Liko ◽  
Povilas Uzdavinys ◽  
Mathieu Coincon ◽  
Jonathan T. S. Hopper ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Gas Phase ◽  
Protein Complexes ◽  
Intact Membrane ◽  
Collisional Cooling ◽  
Membrane Protein Complexes ◽  
Detergent Micelles

Reduced collisional cooling releases intact membrane protein complexes from detergent micelles for unfolding and dissociation studies by mass spectrometry.

Ion Mobility Mass Spectrometry of Two Tetrameric Membrane Protein Complexes Reveals Compact Structures and Differences in Stability and Packing

2010 ◽  
Vol 132 (44) ◽  
pp. 15468-15470 ◽  
Author(s):  
Sheila C. Wang ◽  
Argyris Politis ◽  
Natalie Di Bartolo ◽  
Vassiliy N. Bavro ◽  
Stephen J. Tucker ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Ion Mobility ◽  
Protein Complexes ◽  
Ion Mobility Mass Spectrometry ◽  
Membrane Protein Complexes

scholarly journals YidC family members are involved in the membrane insertion, lateral integration, folding, and assembly of membrane proteins

2004 ◽  
Vol 166 (6) ◽  
pp. 769-774 ◽  
Author(s):  
Ross E. Dalbey ◽  
Andreas Kuhn
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Protein Complexes ◽  
Family Members ◽  
Membrane Insertion ◽  
Conducting Channel ◽  
Energy Devices ◽  
Domains Of Life ◽  
Membrane Protein Complexes ◽  
Sensor Proteins

Members of the YidC family exist in all three domains of life, where they control the assembly of a large variety of membrane protein complexes that function as transporters, energy devices, or sensor proteins. Recent studies in bacteria have shown that YidC functions on its own as a membrane protein insertase independent of the Sec protein–conducting channel. YidC can also assist in the lateral integration and folding of membrane proteins that insert into the membrane via the Sec pathway.

scholarly journals A Novel Chloroplast Super-Complex Consisting of the ATP Synthase and Photosystem I Reaction Center

2019 ◽  
Author(s):  
Satarupa Bhaduri ◽  
Sandeep K Singh ◽  
Whitaker Cohn ◽  
S. Saif Hasan ◽  
Julian P. Whitelegge ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Membrane Protein ◽  
Reaction Center ◽  
Atp Synthase ◽  
Photosystem I ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Native Page ◽  
Membrane Protein Complexes ◽  
Reaction Center Complexes

AbstractSeveral ‘super-complexes’ of individual hetero-oligomeric membrane protein complexes, whose function is to facilitate intra-membrane electron and proton transfer and harvesting of light energy, have been previously characterized in the mitochondrial cristae and chloroplast thylakoid membranes. The latter membrane is reported here to also be the location of an intra-membrane super-complex which is dominated by the ATP-synthase and photosystem I (PSI) reaction-center complexes, defined by mass spectrometry, clear-native PAGE and Western Blot analyses. This is the first documented presence of ATP synthase in a super-complex with the PSI reaction-center located in the non-appressed stromal domain of the thylakoid membrane.

scholarly journals Scratching the surface: native mass spectrometry of peripheral membrane protein complexes

2020 ◽  
Vol 48 (2) ◽  
pp. 547-558 ◽  
Author(s):  
Cagla Sahin ◽  
Deseree J. Reid ◽  
Michael T. Marty ◽  
Michael Landreh
Keyword(s):  
Mass Spectrometry ◽  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Vesicles ◽  
Native Mass Spectrometry ◽  
Integral Membrane Proteins ◽  
Structural Basis ◽  
Lipid Interactions ◽  
Native Ms ◽  
Peripheral Membrane Protein

A growing number of integral membrane proteins have been shown to tune their activity by selectively interacting with specific lipids. The ability to regulate biological functions via lipid interactions extends to the diverse group of proteins that associate only peripherally with the lipid bilayer. However, the structural basis of these interactions remains challenging to study due to their transient and promiscuous nature. Recently, native mass spectrometry has come into focus as a new tool to investigate lipid interactions in membrane proteins. Here, we outline how the native MS strategies developed for integral membrane proteins can be applied to generate insights into the structure and function of peripheral membrane proteins. Specifically, native MS studies of proteins in complex with detergent-solubilized lipids, bound to lipid nanodiscs, and released from native-like lipid vesicles all shed new light on the role of lipid interactions. The unique ability of native MS to capture and interrogate protein–protein, protein–ligand, and protein–lipid interactions opens exciting new avenues for the study of peripheral membrane protein biology.

scholarly journals Evidence for Membrane Complex Assembly in Nanoelectrospray Generated Lipid Bilayers

2019 ◽  
Author(s):  
Matthias Wilm
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayers ◽  
Layered Structure ◽  
Protein Complexes ◽  
Complex Assembly ◽  
Membrane Complex ◽  
Detergent Extraction ◽  
Membrane Protein Complexes

1.AbstractNanoelectrospray can be used to generate a layered structure consisting of bipolar lipids, detergent-solubilized membrane proteins, and glycerol that self-assembles upon detergent extraction into one extended layer of a protein containing membrane. This manuscript presents the first evidence that this method might allow membrane protein complexes to assemble in this process.

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