Difference between revisions of "Team:Bielefeld-CeBiTec/Description"

(adapted text to design)
 
(12 intermediate revisions by one other user not shown)
Line 1: Line 1:
−
{{Team:Bielefeld-CeBiTec/CSS}}
+
{{Team:Bielefeld-CeBiTec/Head}}
 +
{{Team:Bielefeld-CeBiTec/Header}}
 
<html>
 
<html>
−
<head>
 
−
</head>
 
 
<body>
 
<body>
 
<div class="container">
 
<div class="container">
−
<div class="contentbox" style="margin-top: 60px;">
+
        <div class="contentbox">
−
<div class="content style1">
+
<div class="bevel tr"></div>
−
<h2> Expanding the Genetic Code </h2>
+
<div class="content">
−
<h4> Abstract </h4>
+
<h1> Expanding the Genetic Code </h1>
 
<article>
 
<article>
−
With their broad chemical and functional diversity ncAAs provide a variety of promising applications including proteinlabeling, photocaging, structure analysis and specific protein interactions. Therefore, the development of a new iGEM toolkit for the translational incorporation of non-canonical amino acids (ncAAs) in E. coli would be a great contribution to the iGEM community. The site-specific incorporation of ncAAs requires the directed evolution of tRNA and aminoacyl tRNA synthetase pairs, which in turn mediate the introduction of a ncAA for a certain codon. We are especially exploring the application of unnatural base pairs (UBPs) as an expansion of the genetic code. This approach promises an optimal orthogonality to the autologous translation apparatus and a high flexibility concerning the incorporation of multiple ncAAs. We will utilize several systems to achieve a high retention efficiency. As examples for the successful incorporation of non-canonical amino acids we will develop a rapid test for prions and a new chromatography method for a mild elution of proteins.
+
We are exploring the application of unnatural base pairs as an expansion of the genetic code. To prevent loss of unnatural base pairs during replication, we will utilize several systems including CRISPR/Cas9. The expanded genetic code allows for the ribosomal incorporation of multiple non-canonical amino acids (ncAAs) into peptides. With their broad chemical and functional diversity, ncAAs provide a variety of promising applications including protein labeling, photocaging, structure analysis, and specific protein interactions. Therefore, our innovative toolkit for the translational incorporation of ncAAs in E. coli is a valuable contribution to iGEM. Directed evolution of tRNA/aminoacyl-tRNA synthetase pairs enables the site-specific incorporation of ncAAs into peptides. This approach results in an optimal orthogonality to the autologous translation apparatus and a high flexibility concerning the incorporation of multiple ncAAs. As proof of concept, we are developing a rapid test for prions and a new chromatography method for mild protein elution.  
 +
<br>
 +
<p>For more information visit our <b><a href="https://www.researchgate.net/publication/318084694_Expansion_of_the_genetic_code_for_the_translational_incorporation_of_non-canonical_amino_acids">project poster</a></b> on reasearch gate</p>
 
</article>
 
</article>
−
</div>
+
        </div>
−
</div>
+
<div class="bevel bl"></div>
−
</div>
+
    </div>
 +
</div>
 
</body>
 
</body>
 +
<script>
 +
$("#project").addClass("navbar active");
 +
</script>
 
</html>
 
</html>
−
 
−
 
−
 
 
{{Team:Bielefeld-CeBiTec/Footer}}
 
{{Team:Bielefeld-CeBiTec/Footer}}

Latest revision as of 20:51, 27 August 2017

Expanding the Genetic Code

We are exploring the application of unnatural base pairs as an expansion of the genetic code. To prevent loss of unnatural base pairs during replication, we will utilize several systems including CRISPR/Cas9. The expanded genetic code allows for the ribosomal incorporation of multiple non-canonical amino acids (ncAAs) into peptides. With their broad chemical and functional diversity, ncAAs provide a variety of promising applications including protein labeling, photocaging, structure analysis, and specific protein interactions. Therefore, our innovative toolkit for the translational incorporation of ncAAs in E. coli is a valuable contribution to iGEM. Directed evolution of tRNA/aminoacyl-tRNA synthetase pairs enables the site-specific incorporation of ncAAs into peptides. This approach results in an optimal orthogonality to the autologous translation apparatus and a high flexibility concerning the incorporation of multiple ncAAs. As proof of concept, we are developing a rapid test for prions and a new chromatography method for mild protein elution.

For more information visit our project poster on reasearch gate