Team:Freiburg

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Revision as of 00:30, 30 October 2008


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Home

The Team

Project Report

Parts

Modeling

Notebook

Safety

CoLABoration
_welcome!


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The first German team to participate in iGEM ever is back again, providing you with an excellent set of fusion proteins for modular use as [http://partsregistry.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2008&group=Freiburg BioBricks]. This year we are crafting a synthetic receptor kit "made in Black Forest", using DNA-Origami as programmable input device and the complementation of split-fluorophores and -enzymes as readable output.
An [http://parts.mit.edu/igem07/index.php/Freiburg07/report_fusion_parts extension of the standard] BioBrick Pre- and Suffix, developed by iGEM-Team Freiburg 2007, allows in-frame-cloning of proteins without generation of a stop-codon at the "scar", so that we can fuse practically any number of proteins and/or peptides - as you can see in our cloning strategy page. Of course, we want to share this possibility with future iGEM-Teams and have added a new, fully compatible [http://partsregistry.org/Part:BBa_K157000 plasmid] to the registry.

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Project Abstract


Schematical overview of the system

Modular Synthetic Receptor System:

Signaling through membranes is a characteristic of life. Transmembrane proteins control proliferation, differentiation, and cellular response and are key for the formation of multicellular organisms. Controlling such proteins enables modifying cellular behavior and ultimately programming cells at will. The complex rules for transmembrane signaling often require engagement of several proteins in a fine-tuned spatial and temporal manner.

To tap possibilities of transmembrane programming, the Freiburg 2008 iGEM team provides an extensible system comprising an external framework with spatial resolution, a concept for modifying natural receptors, and a modular set of fusion-Biobricks for the construction of synthetic receptors. Spatial resolution in the nanometer scale is provided by DNA-Origami modified with distinct patterns and combinations of ligands. Receptors are decoupled from their natural ligands by fusion with artificial binding domains. The Biobrick collection contains signal sequences, binding domains, transmembrane domains, and effector domains featuring split enzymes and split fluorescent proteins for immediate readout.
For details see the Project Report :

Support

Supporters:

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