Rapid screening of membrane protein activity: electrophysiological analysis of OmpF reconstituted in proteoliposomes

Lab on a Chip ◽  
2008 ◽  
Vol 8 (4) ◽  
pp. 587 ◽  
Author(s):  
Mohamed Kreir ◽  
Cecilia Farre ◽  
Matthias Beckler ◽  
Michael George ◽  
Niels Fertig
Keyword(s):  
Membrane Protein ◽  
Rapid Screening ◽  
Protein Activity ◽  
Electrophysiological Analysis

Liposome chaperon in cell-free membrane protein synthesis: one-step preparation of KcsA-integrated liposomes and electrophysiological analysis by the planar bilayer method

2016 ◽  
Vol 4 (2) ◽  
pp. 258-264 ◽  
Author(s):  
M. Ando ◽  
M. Akiyama ◽  
D. Okuno ◽  
M. Hirano ◽  
T. Ide ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Membrane Protein ◽  
Planar Bilayer ◽  
Electrophysiological Analysis ◽  
One Step ◽  
Free Membrane

Chaperoning functions of liposomes were investigated using cell-free membrane protein synthesis.

scholarly journals Transient Photoinactivation of Cell Membrane Protein Activity without Genetic Modification by Molecular Hyperthermia

ACS Nano ◽  
2019 ◽  
Vol 13 (11) ◽  
pp. 12487-12499 ◽  
Author(s):  
Peiyuan Kang ◽  
Xiaoqing Li ◽  
Yaning Liu ◽  
Stephanie I. Shiers ◽  
Hejian Xiong ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Membrane Protein ◽  
Genetic Modification ◽  
Protein Activity ◽  
Cell Membrane Protein

scholarly journals Cell surface recycling in yeast: mechanisms and machineries

2016 ◽  
Vol 44 (2) ◽  
pp. 474-478 ◽  
Author(s):  
Chris MacDonald ◽  
Robert C. Piper
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Cell Surface ◽  
Mammalian Cells ◽  
Genetic System ◽  
Integral Membrane Protein ◽  
Protein Activity ◽  
Yeast Saccharomyces Cerevisiae ◽  
Central Process

Sorting internalized proteins and lipids back to the cell surface controls the supply of molecules throughout the cell and regulates integral membrane protein activity at the surface. One central process in mammalian cells is the transit of cargo from endosomes back to the plasma membrane (PM) directly, along a route that bypasses retrograde movement to the Golgi. Despite recognition of this pathway for decades we are only beginning to understand the machinery controlling this overall process. The budding yeast Saccharomyces cerevisiae, a stalwart genetic system, has been routinely used to identify fundamental proteins and their modes of action in conserved trafficking pathways. However, the study of cell surface recycling from endosomes in yeast is hampered by difficulties that obscure visualization of the pathway. Here we briefly discuss how recycling is likely a more prevalent process in yeast than is widely appreciated and how tools might be built to better study the pathway.

scholarly journals Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization

2009 ◽  
Vol 66 (1) ◽  
pp. 44-50 ◽  
Author(s):  
Mads Gabrielsen ◽  
Lisa A. Nagy ◽  
Lawrence J. DeLucas ◽  
Richard J. Cogdell
Keyword(s):  
Membrane Protein ◽  
Virial Coefficient ◽  
Protein Crystallization ◽  
Second Virial Coefficient ◽  
Rapid Screening ◽  
Reaction Centre ◽  
Core Complex ◽  
Light Harvesting Complex ◽  
Membrane Protein Crystallization ◽  
Crystallization Conditions

The second virial coefficient, orBvalue, is a measurement of how well a protein interacts with itself in solution. These interactions can lead to protein crystallization or precipitation, depending on their strength, with a narrow range ofBvalues (the `crystallization slot') being known to promote crystallization. A convenient method of determining theBvalue is by self-interaction chromatography. This paper describes how the light-harvesting complex 1–reaction centre core complex fromAllochromatium vinosumyielded single straight-edged crystals after iterative cycles of self-interaction chromatography and crystallization. This process allowed the rapid screening of small molecules and detergents as crystallization additives. Here, a description is given of how self-interaction chromatography has been utilized to improve the crystallization conditions of a membrane protein.

How bilayer lipids affect membrane protein activity

1986 ◽  
Vol 11 (8) ◽  
pp. 331-335 ◽  
Author(s):  
Anthony Carruthers ◽  
Donald L Melchior
Keyword(s):  
Membrane Protein ◽  
Protein Activity

scholarly journals A New Biomimetic Phase of Surfactant Bilayers Maintains Membrane Protein Activity

2013 ◽  
Vol 104 (2) ◽  
pp. 44a
Author(s):  
Vladimir Adrien ◽  
Gamal Rayan ◽  
Myriam Reffay ◽  
Martin Picard ◽  
Arnaud Ducruix ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Activity
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