Difference between revisions of "Team:Shenzhen SFLS/Protein Engineering"

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<a href="https://static.igem.org/mediawiki/2015/9/90/PRdePE_M0_result.txt">Result_M0</a>
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<p><h2><b>3.1 Protein engineering</h2></b></p>
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<p><blockquote>  P185<sup>her2/neu</sup>, member of the HER receptor family, is chosen as the antigen to be mutated in our project. We used several programs to help us have a better overall understanding of the antigen. Since only the extracellular domain can be recognized and bound by an antibody, we would only mutate and express the extracellular domain (ECD). Also, some results below only cover ECD and its mutants.</blockquote></p>
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<img src="https://static.igem.org/mediawiki/2015/c/cd/PRdePE_M0_HDRPH.gif" />
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<center><a href="https://static.igem.org/mediawiki/2015/9/90/PRdePE_M0_result.txt">Numerical_result_of_M0</a></center>
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<img src="https://static.igem.org/mediawiki/2015/d/d2/PRdePE_M0_3rd_structure.png" />
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</br><i><center>Fig 3.1 .Polarity scale of p185her2/neu ECD, predicted by ProtScale, Zimmerman polarity</center></i>
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<img src="https://static.igem.org/mediawiki/2015/5/59/PRdePE_M0_local_quality_estimate.png" />
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<center><img src="https://static.igem.org/mediawiki/2015/c/cd/PRdePE_M0_HDRPH.gif" width="500"/></center>
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</br><i><center>Fig 3.2 .Hydrophobicity scale of p185her2/neu ECD, predicted by ProtScale, Hphob. / Eisenberg et al.</i></center>
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<center><img src="https://static.igem.org/mediawiki/2015/3/3e/PRdePE_M0_2ND_structure.png" width="800"/></center>
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</br><i><center><blockquote><blockquote><blockquote>Fig 3.2 .Hydrophobicity scale of p185her2/neu ECD, predicted by ProtScale, Hphob. / Eisenberg et al.Fig 3.3. Secondary structure and solvent accessibility prediction of p185her2/neu ECD, predicted by PredictProtein. The black scale plate above with numbers indicates the number of residues. Corresponding to the residue numbers, the stripes below the scale plate indicate the secondary structure of the region covered. Blue stripes indicate strand region, while red stripes indicate helix region. Results of the first and second row are respectively predicted by RePROF (new and experimental) and PROFsec (veteran). Results of the third row indicate whether the corresponding region is exposed or buried. Blue stripes indicate that the regions covered are exposed, and yellow stripes indicate that the regions covered are buried.</blockquote></blockquote></blockquote></center></i>
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<center><img src="https://static.igem.org/mediawiki/2015/5/59/PRdePE_M0_local_quality_estimate.png" width="500"/></center>
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Revision as of 12:26, 18 September 2015

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3.1 Protein engineering

P185her2/neu, member of the HER receptor family, is chosen as the antigen to be mutated in our project. We used several programs to help us have a better overall understanding of the antigen. Since only the extracellular domain can be recognized and bound by an antibody, we would only mutate and express the extracellular domain (ECD). Also, some results below only cover ECD and its mutants.

Numerical_result_of_M0

Fig 3.1 .Polarity scale of p185her2/neu ECD, predicted by ProtScale, Zimmerman polarity

Fig 3.2 .Hydrophobicity scale of p185her2/neu ECD, predicted by ProtScale, Hphob. / Eisenberg et al.


Fig 3.2 .Hydrophobicity scale of p185her2/neu ECD, predicted by ProtScale, Hphob. / Eisenberg et al.Fig 3.3. Secondary structure and solvent accessibility prediction of p185her2/neu ECD, predicted by PredictProtein. The black scale plate above with numbers indicates the number of residues. Corresponding to the residue numbers, the stripes below the scale plate indicate the secondary structure of the region covered. Blue stripes indicate strand region, while red stripes indicate helix region. Results of the first and second row are respectively predicted by RePROF (new and experimental) and PROFsec (veteran). Results of the third row indicate whether the corresponding region is exposed or buried. Blue stripes indicate that the regions covered are exposed, and yellow stripes indicate that the regions covered are buried.


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