Difference between revisions of "Template:Team:TU-Eindhoven Wrap HTML"

 
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<html>
 
<html>
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<head>
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<title> iGEM TU Eindhoven </title>
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<link rel="stylesheet" type="text/css"
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href="https://2016.igem.org/Template:TU-Eindhoven/CSS?action=raw&ctype=text/css" />
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<script type="text/javascript" src="https://2016.igem.org/Template:TU-Eindhoven/Javascript?
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action=raw&ctype=text/javascript"></script>
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</head>
 
<div class="Website">
 
<div class="Website">
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<div class="Logo_Panel">
 
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<div class="Logo">
 
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<a target="_blank" href="https://2016.igem.org/Team:TU-Eindhoven">
 
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                          <img id="TU_iGEM_Logo" src="https://static.igem.org/mediawiki/2016/d/d0/TU_Eindhoven--iGEM_Logo.png">
 
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<div class="Title">
 
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[title and motto]
 
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<div class="The_Menu">
 
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<ul class="Menu_List">
 
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<li><a class="active_The_Menu" href="https://2016.igem.org/Team:TU-Eindhoven">Home</a></li>
 
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<li><a href="#">Team</a></li>
 
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<li><a href="#">Project</a></li>
 
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<li><a href="#">Modeling</a></li>
 
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<li><a href="#">Human Practices</a></li>
 
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<li><a href="#">Results</a></li>
 
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<div class="Facebook">
 
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<a target="_blank" href="https://www.facebook.com/iGEMEindhoven2016">
 
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<img id="Facebook_Logo" src="https://static.igem.org/mediawiki/2016/b/ba/Team_TU_Eindhoven_Facebook_Icon.png">
 
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</a>
 
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<div class="iGEM">
 
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<a target="_blank" href="https://2016.igem.org/Main_Page">
 
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<img id="iGEM_Logo" src="https://static.igem.org/mediawiki/2016/c/ca/TU-Eindhoven_iGEM_Logo_2016.png">
 
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<div class="Header_Panel">
 
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    <img class="Image" src="https://static.igem.org/mediawiki/2016/2/21/Team_TU_Eindhoven_Round_Future.png">
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Homepage
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Small molecule mediated scaffolds
 
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<ul class="Side_Menu">
 
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<li><a class="active_Side_Menu" href="https://2016.igem.org/Team:TU-Eindhoven">Homepage</a></li>
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<li><a class="active_Side_Menu" href="https://2016.igem.org/Team:TU-Eindhoven">Home</a></li>
 
</ul>
 
</ul>
 
</div>
 
</div>
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<div class="The_Content">
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            <div id="slideshow-wrap">
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                <input type="radio" id="button-1" name="controls" checked="checked"/>
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                <ul>
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                    <li id="slide1">
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                        <a class="Button" href="https://2016.igem.org/Team:TU-Eindhoven/Description">
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                            Read more
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                        </a>
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                        <div class="Slide_Header" id="Project_title">T14-3-3 based scaffold proteins</div>
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<a href="https://static.igem.org/mediawiki/2016/d/db/T--TU-Eindhoven--Wildtype.png" rel="lightbox">
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                                <img id="Slideshow_Image_1" src="https://static.igem.org/mediawiki/2016/d/db/T--TU-Eindhoven--Wildtype.png">
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                                <p>
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                                    In the emerging field of synthetic biology, many new innovations arise. To use them as efficient and safe as possible, regulation is key. Therefore, iGEM TU Eindhoven is developing new kinds of scaffold proteins, based on 14-3-3 proteins. These scaffold proteins have a wide range of applications in nature and can be used to regulate systems in synthetic biology.
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                        <a class="Button" href="https://2016.igem.org/Team:TU-Eindhoven/Team">
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                        <div class="Slide_Header">Team</div>
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                                <p>
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                                    The iGEM 2016 team of the Eindhoven University of Technology consists of 9 enthusiastic undergraduates of both Biomedical Engineering and Medical Sciences and Technology. Our members work very hard both inside and outside the lab, and have a great time working on our project and learn a lot thanks to iGEM.
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                                </p>
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                        <a class="Button" href="https://2016.igem.org/Team:TU-Eindhoven/Modeling/Rosetta">
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                            Read more
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                        <div class="Slide_Header">Model</div>
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<a href="https://static.igem.org/mediawiki/2016/0/08/T-TU-Eindhoven--Homepage_Model.png" rel="lightbox">
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                                    In order to create new heterodimeric scaffold it is essential to find suitable mutations to create a mutated T14-3-3/CT52 pair that is orthogonal to the wildtype. To find these mutations, The Rosetta software and a self-written protocol was used to determine the yet unknown properties of our newly designed pairs, a model based on Mass-Action and Michaelis-Menten kinetics was developed.
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                                </p>
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                        <a class="Button" href="https://2016.igem.org/Team:TU-Eindhoven/Human_Practices">
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                            Read more
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                        </a>
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                        <div class="Slide_Header">Human Practices </div>
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                        <div class="Slide_Row">
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                            <div class="Column_50">
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                            <a href="https://static.igem.org/mediawiki/2016/6/6e/TUE_HP_frontpage.png" rel="lightbox">
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                                <img id="Slideshow_Image_4" src="https://static.igem.org/mediawiki/2016/6/6e/TUE_HP_frontpage.png">
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                            </a>
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                                <p>
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                                    Three application scenarios were made to investigate the societal impact our scaffold protein might have. To reach out to community an education package was developed. Furthermore, it was investigated how our project can contribute to safety in synthetic biology.
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                                </p>
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                        <a class="Button" href="https://2016.igem.org/Team:TU-Eindhoven/Results/Introduction">
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                            Read more
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                        <div class="Slide_Header">Results</div>
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                                <img id="Slideshow_Image_5" src="https://static.igem.org/mediawiki/2016/thumb/8/8d/TUE_Results_icon.png/438px-TUE_Results_icon.png">
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                                    The performance of CT52 fused NanoBiT fragments was analysed by measuring the luminescence at varying concentrations. The data we acquired in the lab by NanoBit assays for our heterodimers was used in order to verify the quality or our mutations. For each newly found mutation set the functionality of the scaffold and the orthogonality with respect to the wildtype were determined.
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Furthermore a caspase-9 assay was performed to test the activity of caspase-9 after increasing its concentration by T14-3-3.
  
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                            In the emerging field of synthetic biology, many new innovations arise. To use them as efficient and safe as possible, regulation is the key. Therefore, iGEM TU Eindhoven is developing new kinds of scaffold proteins, based on 14-3-3 proteins. These scaffold proteins have a wide range of applications in nature and utilizing this feature they are used to regulate systems in synthetic biology.
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                            Hier nog meer tekst met ergens een linkje of een soort button knop om door te gaan naar die pagina. niet zo'n lelijke zoals bij de vorige pagina.. beetje mooier, zal er nog is naar kijken
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                            The iGEM 2016 team of the Eindhoven University of Technology consists of 9 enthusiastic undergraduates of both Biomedical Engineering and Medical Sciences and Technology. Our members work very hard both inside and outside the lab, and have a great time working on our project and learn a lot thanks to iGEM.
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                            In order to create our heterodimeric scaffold it is essential to find suitable mutations to create a mutated T14-3-3/CT52 pair that is orthogonal to the wildtype. To find these mutations, The Rosetta software and a self-written protocol was used,
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To determine the yet unknown properties of our newly designed pairs, a model based on Mass-Action and Michaelis-Menten kinetics was developed.
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                            Three application scenarios were made to investigate the societal impact our scaffold protein might have. For this, our outreach to society and more, check out the human practices part of our wiki.
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                            The data we acquired in the lab was fit to our model in order to determine the desired properties, showing us how useful our newly designed scaffold is. (WIP).
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                            Hier nog meer tekst met ergens een linkje of een soort button knop om door te gaan naar die pagina. niet zo'n lelijke zoals bij de vorige pagina.. beetje mooier, zal er nog is naar kijken
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Latest revision as of 21:23, 19 October 2016

iGEM TU Eindhoven

Small molecule mediated scaffolds
Welcome to the WIKI of the 2016 iGEM team from Eindhoven University of Technology!
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    T14-3-3 based scaffold proteins

    In the emerging field of synthetic biology, many new innovations arise. To use them as efficient and safe as possible, regulation is key. Therefore, iGEM TU Eindhoven is developing new kinds of scaffold proteins, based on 14-3-3 proteins. These scaffold proteins have a wide range of applications in nature and can be used to regulate systems in synthetic biology.

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    Team

    The iGEM 2016 team of the Eindhoven University of Technology consists of 9 enthusiastic undergraduates of both Biomedical Engineering and Medical Sciences and Technology. Our members work very hard both inside and outside the lab, and have a great time working on our project and learn a lot thanks to iGEM.

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    Model

    In order to create new heterodimeric scaffold it is essential to find suitable mutations to create a mutated T14-3-3/CT52 pair that is orthogonal to the wildtype. To find these mutations, The Rosetta software and a self-written protocol was used to determine the yet unknown properties of our newly designed pairs, a model based on Mass-Action and Michaelis-Menten kinetics was developed.

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    Human Practices

    Three application scenarios were made to investigate the societal impact our scaffold protein might have. To reach out to community an education package was developed. Furthermore, it was investigated how our project can contribute to safety in synthetic biology.

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    Results

    The performance of CT52 fused NanoBiT fragments was analysed by measuring the luminescence at varying concentrations. The data we acquired in the lab by NanoBit assays for our heterodimers was used in order to verify the quality or our mutations. For each newly found mutation set the functionality of the scaffold and the orthogonality with respect to the wildtype were determined. Furthermore a caspase-9 assay was performed to test the activity of caspase-9 after increasing its concentration by T14-3-3.

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