Team:Heidelberg

From 2014.igem.org

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         <p class="normal-middle-text bold">These proteins are extremely <span class="red-text">resistant</span> against
         <p class="normal-middle-text bold">These proteins are extremely <span class="red-text">resistant</span> against
  <span class="red-text">high temperatures</span>, <span class="red-text">pH</span> and <span class="red-text">proteases</span>.</p>
  <span class="red-text">high temperatures</span>, <span class="red-text">pH</span> and <span class="red-text">proteases</span>.</p>
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         <p class="normal-middle-text">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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         <p class="normal-middle-text align-right">We established protein circularization as a <span class="red-text">new<br/>powerful tool</span> for Synthetic Biology and set the foundations to<br />render any protein heat stable.</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 class="large-text">Wondering how we circularize?</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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      <h2 class="middle-text align-right">Let us introduce you to the next generation of bioengineering...</h2>
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       <h2 class="middle-text align-right">COME DISCOVER THE MECHANISM OF SPLIT INTEINS</h2>
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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>Inteins excise themselves out of proteins and in doing so the remaining flanking parts are irreversibly joined</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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         <p>&ndash;an effective mechanism to circularize proteins.</p>
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Revision as of 13:07, 15 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 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.

Placeholder

... and show you the WORLD of
post-translational MODIFCATION

The iGEM Team Heidelberg has developed an intein toolbox for the iGEM community to easily modify your protein in a standarized method.

Our toolbox contains several tools which are PLACEHOLDER. Here you can find out more about our Toolbox.

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.

circular heat-stable
DNMT1

Wouldn´t it be great to amplify DNA in a normal PCR maintaining the epigenetic information coded in methylation patterns?

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. For iGEM 2014 we therefore create a PCR 2.0 with heat-stable DNMT 1 by circularization.

PCR 2.0

circular heat-stable
Xylanase

Xylanase is an important enzyme for the pulp and paper industry.

Bla bla

In future Xylanase could be used for the production of biofuel.

INDUSTRY

LINK it!

Could every protein becomes heat stable by circularization, even if it´s the most complex of all?

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.

In an extensive linker screening our software was improved and calibrated using the lambda phage lysozyme.

CALCULATE it!


After calculating for eleven days and the breakdown of both computational and mental power we decided to spread the modeling of the linkers.

The iGEM Team Heidelberg developed iGEM@home, 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.

As a new tool for the iGEM community this system enables every student team to archieve their modeling without access to big server farms.

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.