Team:ITESM-CEM/CholesterolOxidase
From 2014.igem.org
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- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Modeling | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Modeling">Modeling Proteins</a></sub> |
<sub><a href="https://2014.igem.org/Team:ITESM-CEM/CholesterolOxidase" style="color: #FFF;">Cholesterol Oxidase</a></sub> | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/CholesterolOxidase" style="color: #FFF;">Cholesterol Oxidase</a></sub> | ||
- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Oxoacyl | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Oxoacyl">Oxoacyl Reductase</a></sub> |
- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/Cholesterol">7-Dehydratase</a></sub> |
- | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/EnzymaticKinectics | + | <sub><a href="https://2014.igem.org/Team:ITESM-CEM/EnzymaticKinectics">Enzymatic Kinetics</a></sub> |
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<h2>Cholesterol oxidase</h2> | <h2>Cholesterol oxidase</h2> | ||
- | <p style="text-align: justify; text-justify: inter-word;"> 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.</p><br> | + | <p style="text-align: justify; text-justify: inter-word;"> 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. </p> |
+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/6/61/Colox1.jpg" width="390" height="203" hspace="20"></p><br> | ||
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+ | <p style="text-align: justify; text-justify: inter-word;"> The theoretical dehydratase has 602 aminoacids. The predicted secondary structure is the following. </p> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/0/08/Imagenes_enzimas_modelado-4.jpg" width="625" height="426" hspace="20"></p> | ||
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+ | <h2>Physicochemical Characteristics</h2> | ||
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+ | <p><pie><b>Table 1.</b> Cholesterol oxidase physicochemical characteristics obtained from XTalPred-RF.</pie></p> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/9/99/Tabla_colox.JPG" hspace="20"></p><br> | ||
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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> | ||
+ | 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> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/3/3a/DEHIDRATASA_HIPOT%C3%89TICA-6.jpg" width="390" height="203" hspace="20"></p> | ||
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+ | <p><pie><b>Figure 1.</b> Structural alignment between two variations of the cholesterol oxidase from Chromobacterium sp. The one expressed by the team is highlighted in red, whereas the reference one is marked in blue. </pie></p><br> | ||
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+ | <p class="centeredImage"><img src="https://static.igem.org/mediawiki/2014/c/c5/Colox3.jpg" width="390" height="203" hspace="20"></p> | ||
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+ | <p><pie><b>Figure 2.</b>3D configuration comparison between two variations of the cholesterol oxidase from Chromobacterium sp. The one expressed by the team is left, the reference one is on the right. </pie></p><br> | ||
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Latest revision as of 15:06, 14 October 2014
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