Difference between revisions of "Team:TCU Taiwan/Modeling/Protein structure"
Phoebe chen (Talk | contribs) |
Phoebe chen (Talk | contribs) |
||
| Line 59: | Line 59: | ||
<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="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> | </table> | ||
| Line 68: | Line 68: | ||
<div class="inner"> | <div class="inner"> | ||
<table width="95%" align="center"> | <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> | |
| − | <td width="45%" align="center"><img src="https://static.igem.org/mediawiki/2015/f/f8/2015tcutaiwanModelingwithA1.jpg" align=center width=" | + | |
</tr> | </tr> | ||
</table> | </table> | ||
| Line 93: | Line 92: | ||
<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=" | + | <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="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> | ||
| Line 103: | Line 104: | ||
<table width="95%" align="center"> | <table width="95%" align="center"> | ||
<tr> | <tr> | ||
| − | <td width="45%" align="center"><img src="https://static.igem.org/mediawiki/2015/8/82/2015tcutaiwanModelingepi-1withoutA1.jpg" align=center width=" | + | <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> | ||
Revision as of 15:35, 12 September 2015
|
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. |
|
 |
 |
The first column shows the amino acid sequence 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 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 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. |
|
|
|
| Contact us tcutaiwan@gmail.com No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan |