Team:Heidelberg

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        <h3>iGEM TEAM <span>HEIDELBERG</span> 2014</h3>
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<h3 class="normal-medium-text">iGEM TEAM <span>HEIDELBERG</span> 2014</h3>
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        <h1>THE RING<br />OF <span>FIRE</span></h1>
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<h1 class="very-large-text">THE RING<br />OF <span>FIRE</span></h1>
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        <p>Welcome to the PROTEINS of TOMORROW.<br/>This is the iGEM team Heidelberg‘s wiki page.</p>
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<p> Click <a href="/Team:Heidelberg/Project#Abstract">here</a> to view our abstract.
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<p style="font-size:30px"> Click <a href="/Team:Heidelberg/Project#Abstract">here</a> to view our abstract.
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Scroll down to EXPLORE our project.
Scroll down to EXPLORE our project.
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        <h1 style="text-align:right;"><span class="red-text" style="font-size:1.1em;">CIRCULAR PROTEINS</span></h1>
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<p><span class="larger red-text">Nature</span> has made many curious inventions. One of these are</p>
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        <p><span class="red-text" style="font-size: 1.5em;">Nature</span> has made many curious inventions. One of these are circular proteins, which are conventional peptides that neither have a beginning, nor an ending</p>
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<h1 class="very-large-text red-text bold" style="text-align:right;"><a href="https://2014.igem.org/Team:Heidelberg/Toolbox/Circularization">CIRCULAR PROTEINS</a></h1>
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        <p>Apart from other features, these proteins are extremely stable against
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<p>which are unconventional peptides that neither have a beginning, nor an ending</p><br>
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  high temperatures, pH and proteases.</p>
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<p class="normal-medium-text bold">These proteins are extremely <span class="red-text">resistant</span> against
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        <p style="font-weight:normal; font-size:"25px">We seeked to apply this principle of circularization in Synthetic Biology and create a way of rendering any protein heatstable.</p>
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  <span class="red-text">high temperatures</span>, pH changes and proteases.</p>
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<p class="normal-medium-text align-right">We established protein <a href="/Team:Heidelberg/Toolbox/Circularization"> circularization </a> as a new<br>powerful tool for Synthetic Biology and set the foundations<br>to render any protein heat stable.</p>
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<h1 class="large-text bold">Wondering how we circularize?</h1>
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<h2 class="normal-medium-text align-right bold">Let us introduce you to the next generation of bioengineering...</h2>
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<h2 class="align-right" style="font-size: 40px; font-weight:normal">come DISCOVER the <a href="/Team:Heidelberg/Project/Background">MECHANISM of SPLIT INTEINS</a></h2><br><br>
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<p class=""><span class="larger">Inteins excise themselves out of proteins and in doing so the remaining flanking parts are irreversibly joined</span></p>
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<p><span class="larger">–&nbsp;an effective mechanism to circularize proteins.</span></p>
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<p class="normal-medium-text">But messing with protein structure can be disastrous,<br><span class="medium-text">you can only win with good <a class="bold" href="/Team:Heidelberg/Modeling">MODELING</a>.</span></p><br><br>
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<p class="normal-medium-text"><span>Find out the <span class="bold">EXCITING THEORY</span><br>behind <span class="bold">RIGID LINKERS</span> and their <span class="bold">ANGLES</span></span></p>
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<p><span class="larger">We developed <a href="/Ream:Heidelberg/Software/Linker_Software">CRAUT</a>,<br>
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preserving structure and function.</span></p>
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<p><span class="larger">Look at our extensive wet-lab SCREENING to improve and calibrate our software using <a class="red-text" href="/Team:Heidelberg/Project/Linker_Screening">lambda lysozyme</a>!</span></p>
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<p class="align-right"><span class="larger">As calculations on protein structures are costly<br>we involved the rest of the world with</span></p>
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<h1 class="align-right bold very-large-text dark-red-text"><span style="font-size:1.5em;"><a href="/Team:Heidelberg/Human_Practice/igemathome">iGEM@home</a></span></h1>
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<h3 class="medium-text bold">Empowering science!</h3><br>
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<p class="normal-medium-text"><a href="/Team:Heidelberg/Software/igemathome">NEW PLATFORM</a> for distributed computing.</p>
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<p><span class="larger">Volunteers provide the idle calacity of their home computers.</span></p>
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<p class=""><span class="larger">And, with an established user base with more than <span class="larger red-text">1000</span> computers, we effectively <a href="/Team:Heidelberg/Human_Practice/igemathome" >bring synthetic biology to society</a> in a new way!</span></p>
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<h1 class="large-text">Our Application:</h1>
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<h1 class="dark-grey-text large-text" style="text-align: right;"><span class="medium-large-text">circular <a href="/Team:Heidelberg/Project/PCR_2.0">heat-stable</a></span><br>DNA-methyltransferase</h1>
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<br><br><p><span class="larger">Wouldn´t it be great to amplify DNA preserving the encoded epigenetic information?</span></p>
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<p><span class="larger">This could lead to an ENTIRELY NEW way of performing PCRs with a <a href="/Team:Heidelberg/Project/PCR_2.0">heat stable methyltransferase</a>!</span></p>
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<p>&nbsp;<br /><span class="larger">We'd like to call it</span></p>
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<a href="/Team:Heidelberg/Project/PCR_2.0" class="title-dnmt1">PCR 2.0</a>
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<img src="/wiki/images/5/58/Heidelberg_Toolbox_Circularization.png" id="circ-icon" class="toolbox-icon">&nbsp;&nbsp;CIRCULARIZATION
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<img src="/wiki/images/4/40/Oligomerization.png" id="oligo-icon" class="toolbox-icon">&nbsp;&nbsp;OLIGOMERIZATION
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<img src="/wiki/images/8/87/Heidelberg_Toolbox_Fusion.png" id="fusion-icon" class="toolbox-icon">&nbsp;&nbsp;FUSION
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<img src="/wiki/images/0/04/Heidelberg_Toolbox_Purification.png" id="purification-icon" class="toolbox-icon">&nbsp;&nbsp;PURIFICATION
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<h2 class="normal-medium-text align-right">One more thing.<br>Inteins are capable of much more!</h2>
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<h1 class="medium-large-text align-right bold">We show you the world of</h1>
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<h1 class="medium-text align-right red-text bold" style="font-size: 41px;">post-translational MODIFICATIONS</h1><br><br>
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<p class="align-right "><span class="larger">We created an <a href="/Team:Heidelberg/Project/Toolbox">INTEIN TOOLBOX</a> so you can easily modify your protein in a standardized way.</span></p>
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<p class="align-right"><span class="larger">Take a look at our <a href="/Team:Heidelberg/Parts/RFC">RFC</a>!</span></p>
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      <h1 style="text-align: right; font-size: 3em;" >Let us take you to the next level of bioengineering ...</h1>
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      <h1 style="text-align: center; margin-top:0; font-size:3em; margin-bottom: 15px; font-weight:normal"><span class="light-red-text">USING THE</span> Mechanism <span class="light-red-text">OF</span> SPLIT-INTEINS</h1>
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        <p>Intein splicing is a natural process that excises one part of a protein and leaves the remaining parts irreversibly attached.</p>
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        <p>When attaching split inteins to the ends of a normal protein, the splicing reaction connects the beginning to the ending and forms a circular protein.</p>
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<h1>Who are we?</h1>
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<p>We are the iGEM Team Heidelberg 2014 consisting of 12 highly motivated bachelor and master students studying at Heidelberg University.</p>
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<p>For our project we got great feedback and support from our supervisors.</p>
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<p>Take a look at our <a href="/Team:Heidelberg/Team">Teampage</a>!</p>
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<h1>Thank you!</h1>
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<p>We want thank all people who helped us and supported our work in the lab.</p>
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            <img src="/wiki/images/5/58/Heidelberg_Toolbox_Circularization.png" id="circ-icon" class="toolbox-icon">&nbsp;&nbsp;CIRCULARIZATION
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        <h1 style="text-align: right; font-size: 3em;" >... and show you the  WORLD of <br />
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        <p>The iGEM Team Heidelberg has developed an intein toolbox for the iGEM community to easily modify your protein in a standarized method.</p>
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        <p>Our toolbox contains several tools which are PLACEHOLDER. Here you can find out more about our Toolbox.</p>
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        <p>In addition to that all tools are inducible by light. Using the LOV system we built a solid method for regulation of the intein trans-splicing reaction our toolbox consiting on. Click here to get more informations about Induction.</p>
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        <h1 class="dark-grey-text" style="text-align: right;"><span style="font-size: 0.8em;">circular <span class="red-text">heat-stable</span></span><br>DNMT1</h1>
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        <p>The problem: DNMT 1, an enzyme which is responsible for the establishment and maintenance of the individual methylation pattern of different cell types, is not heat stable.
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          <h1 style="text-align: right; color: black; padding-right: 130px;" ><span style="font-size: 0.8em;">circular <span style="color:white;">heat-stable</span></span><br><span style="font-size:1.3em;">Xylanase</span></h1>
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          <p>Xylanase is an important enzyme for the pulp and paper industry.</p>
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          <p>In future Xylanase could be used for the production of biofuel.</p>
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          <h1 style="text-align: left;" ><span style="font-size:1.3em;">LINK it!</span></h1>
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          <p>Could every protein becomes heat stable by circularization, even if it´s the most complex of all?</p>
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          <p>Circularization is a narrow path between gaining heat-stability and loosing function due to deformation. We developed a linker software, which predict the perfect linker depending on the folding structure of every protein.</p>
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          <p>In an extensive linker screening our software was improved and calibrated using the lambda phage lysozyme.</p>
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            <h1 style="text-align: left; color:#DE4230;" ><span style="font-size:1.5em; font-weights:bold;">CALCULATE it!</span></h1>
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        <p><br/>After calculating for eleven days and the breakdown of both computational and mental power we decided to spread the modeling of the linkers.</p>
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        <p>The iGEM Team Heidelberg developed <a href="/Team:Heidelberg/Software/igemathome">iGEM@home</a>, a software to divide extensive computing task into many packages and to distribute them to many computers. Now over 1,000 volunteers are calculating for us when their computers are idle.</p>
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        <p>As a new tool for the iGEM community this system enables every student team to archieve their modeling without access to big server farms.</p>
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Latest revision as of 23:43, 16 October 2014

iGEM Logo
Ring of fire Image

iGEM TEAM HEIDELBERG 2014

THE RING
OF FIRE

Click here to view our abstract.
Scroll down to EXPLORE our project.

Nature has made many curious inventions. One of these are

CIRCULAR PROTEINS

which are unconventional peptides that neither have a beginning, nor an ending


These proteins are extremely resistant against high temperatures, pH changes and proteases.

We established protein circularization as a new
powerful tool for Synthetic Biology and set the foundations
to render any protein heat stable.

Wondering how we circularize?

Let us introduce you to the next generation of bioengineering...

come DISCOVER the MECHANISM of SPLIT INTEINS



Inteins excise themselves out of proteins and in doing so the remaining flanking parts are irreversibly joined

– an effective mechanism to circularize proteins.

But messing with protein structure can be disastrous,
you can only win with good MODELING.



Find out the EXCITING THEORY
behind RIGID LINKERS and their ANGLES


We developed CRAUT,
a comprehensive software which identifies
the optimal path to connect a protein’s termini
preserving structure and function.

Look at our extensive wet-lab SCREENING to improve and calibrate our software using lambda lysozyme!

As calculations on protein structures are costly
we involved the rest of the world with

iGEM@home

Empowering science!


NEW PLATFORM for distributed computing.

Volunteers provide the idle calacity of their home computers.

And, with an established user base with more than 1000 computers, we effectively bring synthetic biology to society in a new way!

Our Application:

circular heat-stable
DNA-methyltransferase



Wouldn´t it be great to amplify DNA preserving the encoded epigenetic information?

This could lead to an ENTIRELY NEW way of performing PCRs with a heat stable methyltransferase!

 
We'd like to call it

One more thing.
Inteins are capable of much more!

We show you the world of

post-translational MODIFICATIONS



We created an INTEIN TOOLBOX so you can easily modify your protein in a standardized way.

Take a look at our RFC!

Explore all our tools!

Who are we?

We are the iGEM Team Heidelberg 2014 consisting of 12 highly motivated bachelor and master students studying at Heidelberg University.

For our project we got great feedback and support from our supervisors.

Take a look at our Teampage!

Thank you!

We want thank all people who helped us and supported our work in the lab.