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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> | | <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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| − | 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>
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| − | 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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| − | <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 align="center"><h1><span style="font-family:Arial Black;"><font size="6"><font-weight: 700;>Macro Dilution</font></span></h1></td></tr> |
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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"><img src="https://static.igem.org/mediawiki/2015/ f/ f8/ 2015tcutaiwanModelingwithA1. jpg" align=center width=" 80%" title="Result 1"></td> | + | <td width=" 90%" align="center"><img src="https://static.igem.org/mediawiki/2015/ a/ a7/ 2015tcutaiwanThe_peptides_efficiency_of_disinfection. JPG" align=center width=" 60%" title="Result 1"></td> |
| | </tr> | | </tr> |
| − | </table> | + | <tr><td><h1><span style="font-family:Calibri;text-align:justify;"><font size="5"></br> |
| − | </div> | + | |
| − | </div> | + | |
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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>
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| − | The first column shows the amino acid sequence that 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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| | </br></br> | | </br></br> |
| − | </font></span></h1></td></tr> | + | </font></span></h1></td></tr> |
| | </table> | | </table> |
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| − | <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;> Epinicedin-1 pepetide structure analysis</font></span></h1></td></tr>
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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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| + | <tr><td align="center"><h1><span style="font-family:Arial Black;"><font size="6"><font-weight: 700;> Cell </font></span></h1></td></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> | + | |
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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>
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| − | The first column shows the amino acid sequence that 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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| − | </br></br>
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| − | </font></span></h1></td></tr>
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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>
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| − | 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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| − | </br></br>
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| − | </font></span></h1></td></tr>
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