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

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<tr><td align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> About our modeling</font></span></td></tr><tr><td><span style="font-family:Calibri;text-align:justify;"><font size="5">
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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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In order to have more efficient to get our AMPs, we treated signal peptide upstream of the N-terminal of mature antimicrobial peptides. This signal peptide is comes from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the pre-mature peptides go through the periplasmic space, peptidase will identified the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and mature peptide. </br></br>
 
In order to have more efficient to get our AMPs, we treated signal peptide upstream of the N-terminal of mature antimicrobial peptides. This signal peptide is comes from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the pre-mature peptides go through the periplasmic space, peptidase will identified the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and mature peptide. </br></br>
 
To make sure the secretion system is work we attach an Ala at the N-terminal of AMPs. We used protein secondary structure prediction software base on the known peptide structure to analysis whether the attached Ala affect the peptide folding process or not.
 
To make sure the secretion system is work we attach an Ala at the N-terminal of AMPs. We used protein secondary structure prediction software base on the known peptide structure to analysis whether the attached Ala affect the peptide folding process or not.
 
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     <td width="45%" align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 800;> Signiferin</br></font></span><img src="https://static.igem.org/mediawiki/2015/1/17/2015tcutaiwanmodelingsigaddA.JPG" align=center width="80%"  title="with amino acid A"></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="100%"  title="Result 1"></td>
    <td width="45%" align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 800;> with Ala attach </br>N-terminal</br></font></span><img src="https://static.igem.org/mediawiki/2015/2/2a/2015tcutaiwanmodelingdataSigaddA.JPG" align=center width="72%"  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;> Signiferin</br></font></span><img src="https://static.igem.org/mediawiki/2015/6/67/2015tcutaiwanmodelingsigwithoutA.JPG" align=center width="80%"  title="without amino acid A"></td>
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     <td width="45%" align="center"><img src="https://static.igem.org/mediawiki/2015/f/f8/2015tcutaiwanModelingwithA1.jpg" align=center width="100%"  title="Result 1"></td>
     <td width="45%" align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 800;> without Ala attach </br>N-terminal</br><img src="https://static.igem.org/mediawiki/2015/1/12/2015tcutaiwanmodelingdataSigwithoutA.JPG" align=center width="72%"  title="Result 2"></font></span></td>
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<tr><td ><span style="font-family:Calibri;text-align:justify;"><font size="5">The first column shows the amino acid sequence we predict.
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The second column shows that AMPs corresponding secondary structure state are still a-helix.
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The third column shows the probability of correct prediction.
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<tr><td align="center"><span style="font-family:Arial Black;"><font size="7"><font-weight: 700;> Conclusion</font></span></td><td></tr><tr><span style="font-family:Calibri;text-align:justify;"><font size="5"></br></br>
 
  
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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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Through the secondary structure predicted. The result shows whatever Signiferin or Epinecidin-1 the attached of Ala didn’t affect peptide-folding process. They are still a-helix structure.
 
Through the secondary structure predicted. The result shows whatever Signiferin or Epinecidin-1 the attached of Ala didn’t affect peptide-folding process. They are still a-helix structure.
 
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Revision as of 05:07, 8 September 2015

About our modeling

In order to have more efficient to get our AMPs, we treated signal peptide upstream of the N-terminal of mature antimicrobial peptides. This signal peptide is comes from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the pre-mature peptides go through the periplasmic space, peptidase will identified the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and mature peptide.

To make sure the secretion system is work we attach an Ala at the N-terminal of AMPs. We used protein secondary structure prediction software base on the known peptide structure to analysis whether the attached Ala affect the peptide folding process or not.

Conclusion


Through the secondary structure predicted. The result shows whatever Signiferin or Epinecidin-1 the attached of Ala didn’t affect peptide-folding process. They are still a-helix structure.



             
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