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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                                          <a href="https://2010.igem.org/Team:Gothenburg-Sweden/About_us#sts">Students</a>
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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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<td><p>Heat stress denaturases (distorts) proteins, causing weakening of polar  bonds, unfolding, and exposure of hydrophobic  groups. Stress beyond  the cell's tolerance will induce cell death...</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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<p><a href="https://2010.igem.org/Team:Gothenburg-Sweden/About_us">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 the cutting edge technologies available in the field of Synthetic Biology. Our research basically aims to constructing an optical reporter mechanism for cellular stress in yeast by tagging the stress activated SNF1 complex with fluorescent markers.</p>
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<p>The project is executed through two main experimental pathways. Both experimental setups will utilize FRET to visualize the conformational change that is the result of the activation of the SNF1 protein. The first approach consists of creating a fusion protein consisting of the SNF1 protein and two fluorescent proteins, namely EYFP and ECFP. The idea is that when the protein is activated it undergoes a conformational change and a FRET-signal will be visible. 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 will undergo a conformational change that will be visible due to the fluorescent tags.</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 SNF-complex can be moved through a micro-fluidic system, gradually exposing them to an array of substances or a concentration gradient and easily finding out at which concentration or substance that the cells are stressed.</p>
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<p>As of present we have constructed and ordered primers for all fusion proteins that will be tested if they give a FRET signal in yeast. We are also working on 3D models of the fusion protein and will soon be able to present docking predictions with the complex.</p>
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    <li><a href="https://2010.igem.org/Team:Gothenburg-Sweden/Project"
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        <a href="https://2010.igem.org/Team:Gothenburg-Sweden/Project">Description</a>
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        <a href="https://2010.igem.org/Team:Gothenburg-Sweden/Lab_Note">Lab Notes</a>
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        <a href="https://2010.igem.org/Team:Gothenburg-Sweden/Results">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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                              <p>
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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>
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                              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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                                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 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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    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
FUSS

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.

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Chalmers University of Technology, Gothenburg, SWEDEN