Team:Gothenburg-Sweden

From 2010.igem.org

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                              <div class="Title1">Team</div>
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                                          <a href="https://2010.igem.org/Team:Gothenburg-Sweden/About_us#intro">Introduction</a>
 +
                                          <a href="https://2010.igem.org/Team:Gothenburg-Sweden/About_us#cth">CHALMERS</a></li>
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                                          <a href="https://2010.igem.org/Team:Gothenburg-Sweden/About_us#svs">Supervisors</a></li>
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                              <div class="Title1">FUSS</div>
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                                            <a href="#">What's all about?</a>
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                                            <a href="#">Background</a>
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                                            <a href="#">Protein Fusion</a>
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                                            <a href="#">Methods</a>
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                                            <a href="#">Preliminary Results</a>
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<a href="#">Chalmers University of Technology</a>
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        <a href="#">Students</a>
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                                <strong>CHALMERS UNIVERSITY OF TECHNOLOGY, GOTHENBURG</strong></p>  
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                              <p>We are a team of 8 students from Chalmers University of Technology    who will represent Gothenburg, SWEDEN in this year’s iGEM competition.    We have started with a promising idea that combines cutting edge    technologies available in the field of Synthetic Biology. Our research    basically aims to constructing an optical reporter mechanism for    cellular stress by tagging the stress activated SNF1 complex in yeast    with fluorescent markers.<br>  
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                                  <br>
 +
                              The project is performed with two main experimental  pathways: Both  experimental setups will utilize FRET to visualize the  conformational  change that is the result SNF1 activation. The first  approach consists  of fusing fluorescent two proteins, EYFP and ECFP,  with the SNF1  complex. The principal is that when the protein is  activated it  undergoes a conformational change and this should be  indicated by a  change in the FRET-signal. The second approach utilizes  a SAMS-peptide  with fluorescent proteins fused to each end. The  SAMS-peptide will be  phosphorylated by the active SNF1-complex and  undergo a conformational  change that again will be indicated by the  FRET-signal.<br>
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  <br>
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                                The long term ambition of this project it is to use the  results in  the pharmaceutical industry when performing high-throughput  screening  for new substances or finding the correct drug  concentrations to use.  The yeast cells with the modified SNF1-complex  can be moved through a  micro-fluidic system, gradually exposing them  to an array of substances  or a concentration gradient thereby easily  finding at which  concentration or by what substance the cells are  stressed. <br>
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                              As of present we have purified the plasmid backbones that  will be  used together with fusion protein insert to transfect the  yeast cells.  The fusion protein primers has arrived and we will start  working with  the fusion PCR as of this week. We have completed the 3D  models of the  fusion proteins and the results look very promising, we  will soon be  able to present docking predictions with the complex.<br>
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                <div class="Title3">Lab Notes</div>
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                                          <p>11</p>
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                                        </div>
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                                          <div class="newsright"><a href="#">August 11, 2010</a>
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                                          <p> The PCR reaction from yesterday was checked on a gel. α should be ... </p>
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                                          </div>
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                                          <div class="read"><a href="#">read more</a></div>
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                                    <p>Göteborgs-Posten, a major daily newspaper in Sweden with the second largest national circulation, published an article involving the interview with our team...
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                                    <br></p>
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<div class="read"><a href="#">read more</a></div>
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  <div id="myfooter"> <p>  <a href="#">Home</a> | <a href="#">CTH</a> | <a href="#">Sponsors</a> | <a href="#">About Us</a> | <a href="#">Contact Us</a></p> <p>Chalmers University of Technology, Gothenburg, SWEDEN</p>
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<td><p><strong>2010-07-13</strong></p>
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    <p>Göteborgs-Posten, one of Swedens largest newpaper, with over 630 000 readers, had an interview with our team regarding our project today in the Lundberg Laboratory (in cooperation with Gothenburg University). </p></td>
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<td><p>The conceptual idea is to use the conformational change in the SNF1 protein complex to establish a FRET (Förster Resonance Energy Transfer) system for cellular stress detection. There are two chromophores tagged at appropriate locations and upon undergoing the conformational change...</p>
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<p><a href="https://2010.igem.org/Team:Gothenburg-Sweden/Project">Read Full Detail</a></p></td>
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<td><p>We are a team of 8 students from Chalmers University of Technology who    will represent Gothenburg, SWEDEN in this year’s iGEM competition...</p>
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<td><p>to be decided </p>
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<p><a href="https://2010.igem.org/Team:Gothenburg-Sweden/Sponsors">Read Full Detail</a></p></td>
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<td><p>We are a team of 8 students from Chalmers University of Technology  who will represent Gothenburg, SWEDEN in this year’s iGEM competition.  We have started with a promising idea that combines cutting edge  technologies available in the field of Synthetic Biology. Our research  basically aims to constructing an optical reporter mechanism for  cellular stress by tagging the stress activated SNF1 complex in yeast  with fluorescent markers.</p>
+
-
      <p>The project is performed with two main experimental pathways: Both  experimental setups will utilize FRET to visualize the conformational  change that is the result SNF1 activation. The first approach consists  of fusing fluorescent two proteins, EYFP and ECFP, with the SNF1  complex. The principal is that when the protein is activated it  undergoes a conformational change and this should be indicated by a  change in the FRET-signal. The second approach utilizes a SAMS-peptide  with fluorescent proteins fused to each end. The SAMS-peptide will be  phosphorylated by the active SNF1-complex and undergo a conformational  change that again will be indicated by the FRET-signal.</p>
+
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      <p>The long term ambition of this project it is to use the results in  the pharmaceutical industry when performing high-throughput screening  for new substances or finding the correct drug concentrations to use.  The yeast cells with the modified SNF1-complex can be moved through a  micro-fluidic system, gradually exposing them to an array of substances  or a concentration gradient thereby easily finding at which  concentration or by what substance the cells are stressed.</p>
+
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      <p>As of present we have purified the plasmid backbones that will be  used together with fusion protein insert to transfect the yeast cells.  The fusion protein primers has arrived and we will start working with  the fusion PCR as of this week. We have completed the 3D models of the  fusion proteins and the results look very promising, we will soon be  able to present docking predictions with the complex.</p></td>
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  <p><span class="text6">Who we are? </span><br />Left to right: Per Sunnerhagen, Markus Wilhelmsson, Malin Lindén, Karl Almén Burman, Adnan Kadic, Katarina Risö, Peidi Liu, Goutham Vemuri, Lokeshwaran Manoharan, Kemal Sanli, Julia Fransson</p>
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    Synthetic readout of cellular stress</p>
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<p>The cellular stress is sensed  by a key protein called AMP-activated  protein kinase (AMPK). The AMPK protein  complex is conserved among all  eukaryotes, including yeast, plants and humans. </p>
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Latest revision as of 11:56, 3 October 2010

Chalmers University of Technology

Team
Introduction CHALMERS Supervisors Students
FUSS
What's all about? Background Protein Fusion Methods Preliminary Results

CHALMERS UNIVERSITY OF TECHNOLOGY, GOTHENBURG

We are a team of 8 students from Chalmers University of Technology who will represent Gothenburg, SWEDEN in this year’s iGEM competition. We have started with a promising idea that combines cutting edge technologies available in the field of Synthetic Biology. Our research basically aims to constructing an optical reporter mechanism for cellular stress by tagging the stress activated SNF1 complex in yeast with fluorescent markers.

The project is performed with two main experimental pathways: Both experimental setups will utilize FRET to visualize the conformational change that is the result SNF1 activation. The first approach consists of fusing fluorescent two proteins, EYFP and ECFP, with the SNF1 complex. The principal is that when the protein is activated it undergoes a conformational change and this should be indicated by a change in the FRET-signal. The second approach utilizes a SAMS-peptide with fluorescent proteins fused to each end. The SAMS-peptide will be phosphorylated by the active SNF1-complex and undergo a conformational change that again will be indicated by the FRET-signal.

The long term ambition of this project it is to use the results in the pharmaceutical industry when performing high-throughput screening for new substances or finding the correct drug concentrations to use. The yeast cells with the modified SNF1-complex can be moved through a micro-fluidic system, gradually exposing them to an array of substances or a concentration gradient thereby easily finding at which concentration or by what substance the cells are stressed.

As of present we have purified the plasmid backbones that will be used together with fusion protein insert to transfect the yeast cells. The fusion protein primers has arrived and we will start working with the fusion PCR as of this week. We have completed the 3D models of the fusion proteins and the results look very promising, we will soon be able to present docking predictions with the complex.

Home | CTH | Sponsors | About Us | Contact Us

Chalmers University of Technology, Gothenburg, SWEDEN

Retrieved from "http://2010.igem.org/Team:Gothenburg-Sweden"