Team:ITESM-CEM/CholesterolOxidase

From 2014.igem.org

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<p style="text-align: justify; text-justify: inter-word;"> The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.<br>
<p style="text-align: justify; text-justify: inter-word;"> The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.<br>
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Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer. </p> <br><br><br><br><br>
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Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer. </p> <br><br><br>
<p><img src="https://static.igem.org/mediawiki/2014/c/c6/Imagenes_enzimas_modelado-367.jpg" align="left" width="590" height="403" hspace="20"></p> <br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br>
<p><img src="https://static.igem.org/mediawiki/2014/c/c6/Imagenes_enzimas_modelado-367.jpg" align="left" width="590" height="403" hspace="20"></p> <br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br><br>

Revision as of 14:09, 2 October 2014

TEC-CEM | Modeling

ITESM-CEM | Enzy7-K me

Modeling 3325
 

Cholesterol oxidase

This tridimensional model was obtained with the I-TASSER software. It has a - 1.34 C-score which makes it, out of the 5 predicted models, the more plausible to be the actual tridimensional conformation of the protein.




The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following.



Physicochemical characteristics

The following pictures are the structural comparison between two different secuences of the cholesterol oxidase from Chromobacterium sp.
Logically, the results showed a 100% similarity when a BLAST was performed. The only discrepancies found exist on the ends of the protein. Were in figure 4 it can be appreciated a red helix that belongs to the cholesterol oxidase expressed by the iGEM team ITESM.CEM. It is noteworthy that this enzyme works as a monomer.














































 

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