Difference between revisions of "Team:TCU Taiwan/Modeling/Protein structure"
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| + | <img src="https://static.igem.org/mediawiki/2015/1/16/2015tcutaiwanModeling.jpg" width="100%" align="center" /> | ||
| + | |||
<div id="st1" class="st"> | <div id="st1" class="st"> | ||
<div class="inner"> | <div class="inner"> | ||
| − | < | + | <table width="95%" align="center"> |
| − | </font></span> | + | |
| − | </ | + | <tr><td align="justify" ><h1><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> About our modeling</font></span></h1></td></tr> |
| + | <tr><td><h1><span style="font-family:Calibri;text-align:left;"><font size="5"> | ||
| + | To increase efficiency in isolating our AMPs, we introduced a signal peptide upstream of the N-terminal of our AMPs. This signal peptide is obtained from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the fusion peptides enter the periplasmic space, peptidase will identify the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and AMPs. </br></br> | ||
| + | To ensure and verify this process, we have attached an Ala at the N-terminal of AMPs. When applying a protein secondary structure prediction software base on the known peptide structure, we can analyze whether the attached Ala may have an effect on the peptide folding process. | ||
| + | </br></br> | ||
| + | </font></span></h1></td> | ||
| + | </tr> | ||
| + | </table> | ||
</div> | </div> | ||
</div> | </div> | ||
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<div id="st1" class="st"> | <div id="st1" class="st"> | ||
<div class="inner"> | <div class="inner"> | ||
| + | <table width="95%" align="center"> | ||
| + | <tr><td align="left"><h1><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> Signiferin peptide structure analysis</font></span></h1></td></tr> | ||
| + | <tr> | ||
| + | <td width="90%" align="center"><img src="https://static.igem.org/mediawiki/2015/e/ee/2015tcutaiwanModelingwithoutA1.jpg" align=center width="80%" title="Result 1"></td> | ||
| + | </tr> | ||
| + | </table> | ||
| + | </div> | ||
| + | </div> | ||
| + | <div id="st1" class="st"> | ||
| + | <div class="inner"> | ||
<table width="95%" align="center"> | <table width="95%" align="center"> | ||
| − | <td align="center">< | + | |
| − | + | <td width="45%" align="center"><img src="https://static.igem.org/mediawiki/2015/f/f8/2015tcutaiwanModelingwithA1.jpg" align=center width="80%" title="Result 1"></td> | |
| + | </tr> | ||
| + | </table> | ||
| + | </div> | ||
| + | </div> | ||
| + | |||
| + | <div id="st1" class="st"> | ||
| + | <div class="inner"> | ||
| + | <table width="95%" align="center"> | ||
| + | <tr><td><h1><span style="font-family:Calibri;text-align:justify;"><font size="5"></br> | ||
| + | The first column shows the amino acid sequence that we predict. | ||
| + | The second column shows that AMPs corresponding secondary structure state are still a-helix. | ||
| + | The third column shows the probability of correct prediction. | ||
| + | </br></br> | ||
| + | </font></span></h1></td></tr> | ||
</table> | </table> | ||
</div> | </div> | ||
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<table width="95%" align="center"> | <table width="95%" align="center"> | ||
<tr> | <tr> | ||
| − | + | <tr><td align="left"><h1><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> Epinicedin-1 pepetide structure analysis</font></span></h1></td></tr> | |
| − | + | <tr> | |
| + | <td width="45%" align="center"><img src="https://static.igem.org/mediawiki/2015/8/82/2015tcutaiwanModelingepi-1withoutA1.jpg" align=center width="80%" title="Result 4"></td> | ||
</tr> | </tr> | ||
</table> | </table> | ||
| Line 67: | Line 104: | ||
<table width="95%" align="center"> | <table width="95%" align="center"> | ||
<tr> | <tr> | ||
| − | + | <td width="90%" align="center"><img src="https://static.igem.org/mediawiki/2015/1/10/2015tcutaiwanigemModelingepi-1withA1.jpg" align=center width="80%" title="Result 3"></td> | |
| − | + | ||
</tr> | </tr> | ||
</table> | </table> | ||
</div> | </div> | ||
</div> | </div> | ||
| + | |||
<div id="st1" class="st"> | <div id="st1" class="st"> | ||
<div class="inner"> | <div class="inner"> | ||
<table width="95%" align="center"> | <table width="95%" align="center"> | ||
| − | + | <tr><td><h1><span style="font-family:Calibri;text-align:justify;"><font size="5"></br> | |
| − | + | The first column shows the amino acid sequence that we predict. | |
| − | + | The second column shows that AMPs corresponding secondary structure state are still a-helix. | |
| + | The third column shows the probability of correct prediction. | ||
| + | </br></br> | ||
| + | </font></span></h1></td></tr> | ||
| + | </table> | ||
| + | </div> | ||
| + | </div> | ||
| + | |||
| + | |||
| + | <div id="st1" class="st"> | ||
| + | <div class="inner"> | ||
| + | <table width="95%" align="center"> | ||
| + | |||
| + | <tr><td align="center"><h1><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> Conclusion</font></span></h1></td></tr> | ||
| + | <tr><td><h1><span style="font-family:Calibri;text-align:justify;"><font size="5"></br> | ||
| + | Through the analysis of the peptide secondary structure and confirmation of the -helix structure, the results show whether Ala is attached to Signiferin or Epinecidin-1, the peptide did not affect the peptide folding process. process. | ||
| + | </br></br> | ||
| + | </font></span></h1></td></tr> | ||
</table> | </table> | ||
</div> | </div> | ||
Latest revision as of 16:38, 18 September 2015
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To increase efficiency in isolating our AMPs, we introduced a signal peptide upstream of the N-terminal of our AMPs. This signal peptide is obtained from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the fusion peptides enter the periplasmic space, peptidase will identify the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and AMPs. To ensure and verify this process, we have attached an Ala at the N-terminal of AMPs. When applying a protein secondary structure prediction software base on the known peptide structure, we can analyze whether the attached Ala may have an effect on the peptide folding process. |
|
 |
 |
The first column shows the amino acid sequence that we predict. The second column shows that AMPs corresponding secondary structure state are still a-helix. The third column shows the probability of correct prediction. |
|
 |
 |
The first column shows the amino acid sequence that we predict. The second column shows that AMPs corresponding secondary structure state are still a-helix. The third column shows the probability of correct prediction. |
|
Through the analysis of the peptide secondary structure and confirmation of the -helix structure, the results show whether Ala is attached to Signiferin or Epinecidin-1, the peptide did not affect the peptide folding process. process. |
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| Contact us tcutaiwan@gmail.com No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan |