Difference between revisions of "Team:Vilnius-Lithuania/Collection"

 
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<h1 class="text-wall-heading">Part Collection</h1>
 
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                 <p class="c1"><span class="c12 c8">BBa_K262<a href="http://parts.igem.org/Part:BBa_K2622047"> BBa_2622047</a> 2047</span></p>
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                 <p class="c1"><span class="c12 c8"><a href="http://parts.igem.org/Part:BBa_K2622047"> BBa_2622047</a> </span></p>
 
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                 <p class="c1"><span class="c12 c8">OmpA full</span></p>
 
                 <p class="c1"><span class="c12 c8">OmpA full</span></p>
 
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               <td class="c15" colspan="1" rowscp<a href="http://parts.igem.org/Part:BBa_K2622038"> BBa_2622038</a> an="1">
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                 <p class="c1"><span class="c12 c8">Full lenght outer transmembrane protein A (OmpA)</span></p>
 
                 <p class="c1"><span class="c12 c8">Full lenght outer transmembrane protein A (OmpA)</span></p>
 
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Latest revision as of 20:35, 4 November 2018

Part Collection

Irreplaceable Force

We have created a large and extensive part collection in which each piece has a different specific function, however they all consolidate for a common purpose of creating a liposome-based synthetic biology platform for membrane protein research. The collection comprises cellular MP integration machinery, target membrane proteins, and a unique chaperone. Guide RNAs introduce genetic modifications to nascent ribosome proteins for purification and further ribosome anchoring to nickel-chelating lipids of liposome membrane. Synthetic RNA thermometers act as a user-controllable mechanism for regulation of target protein expression and high-yield synthesis in an inducible temperature range. Thermoswitches elegantly complement the function of BAM complex which facilitates membrane-assembly of beta-barrel bearing proteins. Our target membrane proteins are fused with Mistic protein for a superior integration into the membrane. Additionally, MPs of our choice expose designated antibodies on the surface of the liposome.

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