Team:Berkeley/Project/Zippers

From 2012.igem.org

(Difference between revisions)
Line 64: Line 64:
<div class="col1" align="justify">
<div class="col1" align="justify">
<p>
<p>
-
Protein interaction domains (coiled coils, PDZ, SH3, GBD, etc) have been used by synthetic biologists to oligomerize or localize proteins. In particular, they have been applied to both scaffolding and signaling applications with impressive results. However, the limited number and diversity of well-characterized, orthogonal protein interaction domains restricts the complexity of systems that can be designed. The problem of screening for protein-protein interactions arises
+
Protein interaction domains (coiled coils, PDZ, SH3, GBD, etc) have been used by synthetic biologists to oligomerize or localize proteins. In particular, they have been applied to both scaffolding and signaling applications with impressive results. However, the limited number and diversity of well-characterized, orthogonal protein interaction domains restricts the complexity of systems that can be designed. Current screening methods for protein-protein interactions (such as transcription-driven GFP expression in yeast 2-hybrid systems) are not high throughput to analyze large library sizes of protein interaction pairs.  However, with the utilization of MiCodes and microscopy’s ability to record spatial information, we are able to design an assay to screen for orthogonal protein-protein interaction pairs. 
-
 
+
</p>
</p>
</div>
</div>

Revision as of 01:22, 3 October 2012

header
iGEM Berkeley iGEMBerkeley iGEMBerkeley

Mercury

Protein interaction domains (coiled coils, PDZ, SH3, GBD, etc) have been used by synthetic biologists to oligomerize or localize proteins. In particular, they have been applied to both scaffolding and signaling applications with impressive results. However, the limited number and diversity of well-characterized, orthogonal protein interaction domains restricts the complexity of systems that can be designed. Current screening methods for protein-protein interactions (such as transcription-driven GFP expression in yeast 2-hybrid systems) are not high throughput to analyze large library sizes of protein interaction pairs. However, with the utilization of MiCodes and microscopy’s ability to record spatial information, we are able to design an assay to screen for orthogonal protein-protein interaction pairs.


Why we bound mKate to bait and PTS1 to prey. Includes images showing preliminary results.


Our home run experiment with 40 bait and 40 prey.