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Team:Heidelberg/testing/Frontpage
From 2014.igem.org
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<h1 style="text-align: left;" ><span style="font-size:1.3em;">LINK it!</span></h1> | <h1 style="text-align: left;" ><span style="font-size:1.3em;">LINK it!</span></h1> | ||
<p>Could every protein becomes heat stable by circularization even if it´s the complexest of all?</p> | <p>Could every protein becomes heat stable by circularization even if it´s the complexest of all?</p> | ||
Revision as of 11:41, 9 October 2014
iGEM TEAM HEIDELBERG 2014
THE RING
OF FIRE
Dieser Text soll reinhauen.
Am besten sollte er richtig gut sein!
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 I, 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 I by circularization.
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.
LINK it!
Could every protein becomes heat stable by circularization even if it´s the complexest of all?
Circularization is a narrow path between heat-stability and loss of function due to deformation. We developed a linker software, which predict the most suitable 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.
