Difference between revisions of "Team:TCU Taiwan/Modeling"

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<table width="95%"  align="center">
 
<table width="95%"  align="center">
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<td align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> About our modeling</br></br></br></br></br></br></br></font></span></td>
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<tr><td align="center"><h1><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> About our modeling</font></span></h1></td></tr>
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<tr><td><h1><span style="font-family:Calibri;text-align:left;"><font size="5">
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To increase efficiency in isolating our AMPs, we introduced a signal peptide upstream of the N-terminal of mature antimicrobial peptides. This signal peptide is obtained from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the premature peptides enter the periplasmic space, peptidase will identify the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and mature peptide. </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.
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</br></br>
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  <div class="inner">
 
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<table width="95%"  align="center">
 
<table width="95%"  align="center">
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<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>
 
   <tr>
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     <td width="45%" align="center"><img src="#" align=center width="72%"  title="Result 1"></td>
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     <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>
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    <td width="45%" align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 800;> Result 1</br></br></br></br></br></br></br></font></span></td>
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   </tr>   
 
   </tr>   
 
</table>
 
</table>
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  <div class="inner">
 
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<table width="95%"  align="center">
 
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    <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>
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  </tr> 
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</table>
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</div>
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<div id="st1" class="st">
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<div class="inner">
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<table width="95%"  align="center">
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<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.
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</br></br>
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</font></span></h1></td></tr>
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</table>
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</div>
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</div>
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<div id="st1" class="st">
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<div class="inner">
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<table width="95%"  align="center">
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  <tr>
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<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>
 
   <tr>
−
<td width="45%" align="center"><img src="#" align=center width="72%"  title="Result 2"></td>
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  <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>
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    <td width="45%"  align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 800;> Result 2</br></br></br></br></br></br></br></font></span></td>
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   </tr>   
 
   </tr>   
 
</table>
 
</table>
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</div>
 
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<div id="st1" class="st">
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<div class="inner">
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<table width="95%"  align="center">
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  <tr>
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<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>
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  </tr> 
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</table>
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</div>
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</div>
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<div id="st1" class="st">
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<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>
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</table>
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</div>
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</div>
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<div id="st1" class="st">
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<div class="inner">
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<table width="95%"  align="center">
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<tr><td align="center"><h1><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> Conclusion</font></span></h1></td></tr>
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<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>
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</font></span></h1></td></tr>
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Revision as of 02:26, 18 September 2015

About our modeling

To increase efficiency in isolating our AMPs, we introduced a signal peptide upstream of the N-terminal of mature antimicrobial peptides. This signal peptide is obtained from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the premature peptides enter the periplasmic space, peptidase will identify the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and mature peptide.

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.

Signiferin peptide structure analysis


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.

Epinicedin-1 pepetide structure analysis


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.

Conclusion


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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 tcutaiwan@gmail.com
No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan