Team:Berkeley Wetlab

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<big><font size="5" face="Book Antiqua"> Abstract</font> </big> <br>
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Cell surface display in e. Coli tethers proteins to the outer membrane to localize them to the extracellular environment.  While this form of localization has allowed many novel functions to be engineered into e. Coli, work within this space relies on a trial and error approach rather than design principles.  We worked to create a foundation of research which would make possible the rational design of cell surface display systems in e. ColiA combinatorial approach was used to compare the ability of different display proteins to functionally display representative members of different protein classes.  This required the development and implementation of an automated assembly method able to construct the large number of devices necessary to draw meaningful conclusions about design within this space.   
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Cell surface display in ''E. coli'' tethers proteins to the outer membrane in order to localize them to the extracellular environment.  While this form of localization has allowed many novel functions to be engineered into ''E. coli'', work within this space relies on a trial and error approach rather than design principles.  We worked to create a foundation of research which would make the rational design of cell surface display systems in ''E. coli''  possibleWe used a combinatorial approach to compare the ability of different display proteins to display different classes of functional proteins.  This required the development and implementation of an automated assembly method able to construct the large number of devices necessary to draw meaningful conclusions about design within this space.   
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<center><font size="5" face="Book Antiqua">Our Team</font></center> <br>
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Latest revision as of 19:14, 21 October 2009


Display-o-matic2.png

Abstract
Cell surface display in E. coli tethers proteins to the outer membrane in order to localize them to the extracellular environment. While this form of localization has allowed many novel functions to be engineered into E. coli, work within this space relies on a trial and error approach rather than design principles. We worked to create a foundation of research which would make the rational design of cell surface display systems in E. coli possible. We used a combinatorial approach to compare the ability of different display proteins to display different classes of functional proteins. This required the development and implementation of an automated assembly method able to construct the large number of devices necessary to draw meaningful conclusions about design within this space.




Our Team

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Acknowledgements
We thank our wonderful advisers: Chris Anderson, Terry Johnson, and Lane Weaver for their guidance and support. We also thank our generous sponsors:


Berkeleyinvitrogen.jpg Berkeleynsf.jpg Berkeleyqbs.jpg Berkeleysynberg.png