Team:Gothenburg-Sweden

From 2010.igem.org

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                                            <a href="#">Protein Fusion</a>
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                <h2><a href="http://www.metamorphozis.com/" id="metamorph">chalmers tekniska högskolan </a></h2>
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                            <span>iGEM team - Gothenburg, Chalmers University of Technology </span> <br />
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<a href="#">Chalmers University of Technology</a>
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                            We are a team of 8 students from Chalmers University of Technology who   will represent Gothenburg, SWEDEN in this year’s IGEM competition. IGEM  stands for International Genetically Engineered Machines and is a  competition based upon interdisciplinary collaboration of students on a  Synthetic Biology project. The competition is held in MIT, Boston and is  open to all universities from various countries world-wide. There are  180 teams participating this year with about 2000 students in total. We   have started with a promising idea that combines the cutting edge   technologies available in the field of Synthetic Biology. Our research   basically includes the specification and designing of a biological  system followed by the application of Molecular Biology techniques to  build and test it experimentally. The premise of the competition for the   students will be to learn engineering approaches and tools to organize,  model, and assemble complex systems and to immerse themselves in  applied molecular biology. In the project, we are investigating a   biological phenomenon that is a part of insulin uptake mechanism, widely   studied in Diabetic research. Our endeavor in the study is to visualize   a part of the mechanism by making use of the Nobel Prize winning idea   of the Green Fluorescent Proteins (GFPs). Hopefully, the project will   provide us with auspicious outcomes to further improve the study of the  disease.<br />
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        <a href="#">Supervisors</a>
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                        <h1>Project - Synthetic readout of cellular stress </h1>
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    <li><a href="https://2010.igem.org/Team:Gothenburg-Sweden/Sponsors">Sponsors</a></li>
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                            <img src="images/cell stress.jpg" alt="" width="260" height="180" class="img" />                          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. The <strong>cellular stress response</strong> (<strong>heat-shock response</strong>) protects  organisms from damage resulting from environmental stressors such as heat, UV  light, trace metals, and xenobiotics. Stress genes are activated to rapidly  synthesize <strong>stress proteins</strong>, which are highly conserved in biological evolution and play similar roles in organisms  from bacteria to humans.
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    <li><a href="https://2010.igem.org/Team:Gothenburg-Sweden/Contact">Contact Us</a></li>
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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. In humans this is the target of most anti-diabetic drugs in the market today  and is also implicated in many other metabolic disorders such as obesity and  atherosclerosis and also in developmental processes such as cell cycle and  ageing, etc. In yeast, this protein is called SNF1 and to use the conformational change in the SNF1 complex to establish a FRET (Förster  Resonance Energy Transfer) system. </p>
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                        <h1>Contact Information </h1>
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                        <p>&nbsp;</p>
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                        <p>iGEM team Gothenburg:</p>
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                                <strong>CHALMERS UNIVERSITY OF TECHNOLOGY, GOTHENBURG</strong></p>  
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                        <p>Chalmers University of Technology</p>
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                        <p>Email: xxxx@xxxx.xxx</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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                        <p>&nbsp; </p>
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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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                        <h1>Recently News</h1>
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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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                            <li><span class="dat">06-11-2010</span> <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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                            <li ><span class="dat">07-11-2010</span> <br />
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                                          <p>11</p>
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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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                                    <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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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

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