Team:Heidelberg

From 2014.igem.org

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             <p class="larger align-right">As calculations on protein structures are costly<br />we involved the rest of the world with</p>
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             <h1 class="very-large-text red-text">iGEM@home</h1>
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         <h3 class="normal-medium-text">Empowering science!</h3>
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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>NEW PLATFORM for distributed computing.</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>Volunteers provide the idle calacity of their home computers.</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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         <p>And, with an established user base with more than <span class="larger red-text">1000</span> computers, we effectively bring synthetic biology to society in a new way</p>
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Revision as of 14:28, 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

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

... 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

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

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.

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