Team:Freiburg/Description

From 2011.igem.org

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(Part design)
(Part design)
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This protein can be used to complex Nickel or Cobalt. Histidines are positioned in such a way, that they can coordinate the ions
This protein can be used to complex Nickel or Cobalt. Histidines are positioned in such a way, that they can coordinate the ions
from two to four orthogonally oriented directions. Free binding sites of the ions are then exposed, so that a His-tagged protein can attach to them. This protein can be used to complex up to 4 nickel or cobalt ions.  
from two to four orthogonally oriented directions. Free binding sites of the ions are then exposed, so that a His-tagged protein can attach to them. This protein can be used to complex up to 4 nickel or cobalt ions.  
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The spelling design of the protein is of a particular interest, too.  
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The underlying design of the protein is of a particular interest, too.  
LRRs are highly conserved motifs throughout evolution. They appear in all kingdoms of life in almost every thinkable role (ligases, receptors, toxins etc.). Their core is highly conserved and provides a very stable backbone, while the non-conserved aminoacids are almost freely interchangeable.  
LRRs are highly conserved motifs throughout evolution. They appear in all kingdoms of life in almost every thinkable role (ligases, receptors, toxins etc.). Their core is highly conserved and provides a very stable backbone, while the non-conserved aminoacids are almost freely interchangeable.  
Here we investigated an optimal set of non-conserved aminoacids by analysing large sets of similar proteins and databases. You can use this piece of work as a template to design your own protein and give it any function you like, by simply interchanging aminoacids and fusing other domains on the N or C termini. To guarantee proper folding and to shield off the hydrophobic core, a well studied fragment of an LRR protein coming from hagfish was used. This efficiency of this technique was proven before.(Schmidt 2010). To find out the most likely folding, we designed many different protein sequences, trying out a variety of sets of non coding aminoacids for the LRR and submitted these to the I-TASSER structure prediction  
Here we investigated an optimal set of non-conserved aminoacids by analysing large sets of similar proteins and databases. You can use this piece of work as a template to design your own protein and give it any function you like, by simply interchanging aminoacids and fusing other domains on the N or C termini. To guarantee proper folding and to shield off the hydrophobic core, a well studied fragment of an LRR protein coming from hagfish was used. This efficiency of this technique was proven before.(Schmidt 2010). To find out the most likely folding, we designed many different protein sequences, trying out a variety of sets of non coding aminoacids for the LRR and submitted these to the I-TASSER structure prediction  

Revision as of 17:06, 21 September 2011


This is the wiki page
of the Freiburger student
team competing for iGEM 2011.
Thank you for your interest!