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Membrane Protein Solutions

Amphipols & Detergents
   



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   (1) Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions[1]
   


Amphipols are small polymers that enable handling of membrane proteins in detergent-free aqueous solution as though they were soluble proteins. They form hydrophilic complexes with the protein and allow working without detergents. The short Amphipol A8-35 is highly soluble in water and tightly binds to the transmembrane domains through its hydrophobic moieties[2]. A8-35 facilitates stability and biological activity of solubilized membrane proteins[3] and is especially useful for sample preparation in Cryo-EM[4-7].


The amphiphilic polymer Amphipol A8-35 consists of a strong hydrophilic backbone grafted with hydrophobic chains[1].

   
   (2) The Classics: Detergents that keep membrane proteins soluble
   


Finding a suitable detergent that keeps a membrane protein in solution remains largely a trial and error process however, for growing crystals of membrane proteins the JBScreen Detergents has been developed.

Its 96 detergents were thoroughly selected from published crystallization trials in which they were shown to efficiently solubilize the membrane protein without shielding surface regions that are involved in crystal contacts. Discover JBScreen Detergents and receive 20 % discount on JBScreen Detergents HTS (Cat. No. CS-525) !*

* Valid until May 12th, 2017, please indicate the code "Detergents promo" when placing your order!


References:
[1] Tribet et al. (1996) Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions PNAS 93:15047.
[2] Zoonens et al. (2014) Amphipols for Each Season. J. Membrane Biol. 247:759.
[3] Popot et al. (2011) Amphipols From A to Z. Annu. Rev. Biophys. 40:379.
[4] Chen et al. (2016) Structure of the STRA6 receptor for retinol uptake. Science 353:887.
[5] Zubcevic et al. (2016) Cryo-Electron Microscopy of the Trpv2 Ion Channel. Nat. Struct. Mol. Biol. 23:180.
[6] Bai et al. (2015) Sampling the conformational space of the catalytic subunit of human gamma-secretase. DOI 10.7554/eLife.11182.
[7] Althoff et al. (2011) Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J. 30:4652.

   
   
   
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