Difference between revisions of "Team:TCU Taiwan/Modeling/Protein structure"
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<table width="95%" align="center"> | <table width="95%" align="center"> | ||
− | <tr><td align=" | + | <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: | + | <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 | + | 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> | </br></br> | ||
</font></span></h1></td> | </font></span></h1></td> | ||
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<div class="inner"> | <div class="inner"> | ||
<table width="95%" align="center"> | <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> | <tr> | ||
− | <td width="90%" align="center"><img src="https://static.igem.org/mediawiki/2015/e/ee/2015tcutaiwanModelingwithoutA1.jpg" align=center width=" | + | <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> | </tr> | ||
+ | </table> | ||
+ | </div> | ||
+ | </div> | ||
+ | |||
+ | <div id="st1" class="st"> | ||
+ | <div class="inner"> | ||
+ | <table width="95%" 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> | ||
</div> | </div> | ||
</div> | </div> | ||
+ | |||
+ | <div id="st1" class="st"> | ||
+ | <div class="inner"> | ||
+ | <table width="95%" align="center"> | ||
+ | <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> | ||
+ | </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> | ||
+ | </div> | ||
+ | </div> | ||
+ | |||
<div id="st1" class="st"> | <div id="st1" class="st"> | ||
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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> | <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> | <tr><td><h1><span style="font-family:Calibri;text-align:justify;"><font size="5"></br> | ||
− | Through the secondary structure | + | 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> | </br></br> | ||
</font></span></h1></td></tr> | </font></span></h1></td></tr> |
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. |
Contact us tcutaiwan@gmail.com No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan |