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

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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 -helix.
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The third column shows the probability of correct prediction.
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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="100%"  title="Result 3"></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="100%"  title="Result 4"></td>
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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 -helix.
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The third column shows the probability of correct prediction.
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Revision as of 05:50, 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.


The first column shows the amino acid sequence we predict. The second column shows that AMPs corresponding secondary structure state are still -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 -helix. The third column shows the probability of correct prediction.

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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 tcutaiwan@gmail.com
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