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
2015 ◽  
Vol 51 (85) ◽  
pp. 15582-15584 ◽  
Author(s):  
Michael Landreh ◽  
Idlir Liko ◽  
Povilas Uzdavinys ◽  
Mathieu Coincon ◽  
Jonathan T. S. Hopper ◽  
...  

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


2015 ◽  
Vol 24 (8) ◽  
pp. 1292-1300 ◽  
Author(s):  
Albert Konijnenberg ◽  
Ludovic Bannwarth ◽  
Duygu Yilmaz ◽  
Armağan Koçer ◽  
Catherine Venien-Bryan ◽  
...  

2014 ◽  
Vol 136 (49) ◽  
pp. 17010-17012 ◽  
Author(s):  
Shahid Mehmood ◽  
Julien Marcoux ◽  
Jonathan T. S. Hopper ◽  
Timothy M. Allison ◽  
Idlir Liko ◽  
...  

2010 ◽  
Vol 132 (44) ◽  
pp. 15468-15470 ◽  
Author(s):  
Sheila C. Wang ◽  
Argyris Politis ◽  
Natalie Di Bartolo ◽  
Vassiliy N. Bavro ◽  
Stephen J. Tucker ◽  
...  

2019 ◽  
Author(s):  
Satarupa Bhaduri ◽  
Sandeep K Singh ◽  
Whitaker Cohn ◽  
S. Saif Hasan ◽  
Julian P. Whitelegge ◽  
...  

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.


2019 ◽  
Vol 400 (7) ◽  
pp. 813-829 ◽  
Author(s):  
Julian Bender ◽  
Carla Schmidt

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.


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