Difference between revisions of "Team:BostonU/Home"

Line 601: Line 601:
 
                             <img class="DCMationgif" style="margin-left:5%;" src="https://static.igem.org/mediawiki/2014/8/81/DCMation1.png" alt="" onclick="javascript:(this.src==&quot;https://static.igem.org/mediawiki/2014/8/81/DCMation1.png&quot;?this.src=&quot;https://static.igem.org/mediawiki/2014/e/e2/OxigemDCMationgif.gif&quot;:&quot;&quot;)" width="90%" align="middle">
 
                             <img class="DCMationgif" style="margin-left:5%;" src="https://static.igem.org/mediawiki/2014/8/81/DCMation1.png" alt="" onclick="javascript:(this.src==&quot;https://static.igem.org/mediawiki/2014/8/81/DCMation1.png&quot;?this.src=&quot;https://static.igem.org/mediawiki/2014/e/e2/OxigemDCMationgif.gif&quot;:&quot;&quot;)" width="90%" align="middle">
  
−
                            University of Oxford’s first iGEM team presents: DCMation, a novel bioremediation approach whose applications are limited only by the versatility of bacterial metabolism. OxiGEM are tackling environmental pollution by developing a user-friendly device for the detection &amp; degradation of the hazardous yet indispensable solvent dichloromethane (DCM), to illustrate.
+
                         
−
                            <br>
+
−
                            Inspired by the DCM degradation pathway of <font style="font-style: italic;">M. extorquens</font> DM4, our project is driven and refined by the dialogue between modelling simulations and experimental data. Bioremediation is optimised by expressing the DCM degrading system in host strains, along with microcompartments to accelerate the reaction and minimise toxic intermediates. Our biosensor is tuned to our characterisation and improvements of the catalytic efficiency of the system, while incorporation of the bacteria into novel diffusion-limiting biopolymeric beads ensures safe and rapid degradation.
+
−
                            <br>
+
−
                            This all-round modular design and scalability make DCMation ideal for extension to the disposal of many harmful substances. Explore our wiki for more!
+
−
 
+
−
 
+
 
                         </div>
 
                         </div>
 
                     </div>
 
                     </div>

Revision as of 13:42, 14 July 2015

Simple 2 column CSS layout, final layout | 456 Berea Street

Our Project

The goal of our team this summer is to create an efficient and widely applicable workflow for splitting proteins. By splitting proteins and fusing each half to a drug-inducible domain, scientists can gain temporal control over protein expression. Using our workflow, the proteins will be translated into two inert halves that are each fused to domains that bind in the presence of an inducer drug. By introducing the drug into the system, the two inert protein halves will come together and for a fully functioning protein. In this way, scientists can further increase their control over protein function. The two types of proteins we will be testing our workflow on are the large serine integrase family and saCAS9. These proteins harness powerful mechanisms that have significant applications in the future of synthetic biology. By using our workflow, we hope to increase scientists understanding of these proteins and also provide a mechanism for increasing temporal control.