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"> | + | <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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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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| − | <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"> | + | <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> |
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. | ||
Revision as of 04:24, 8 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. |
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| 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. |
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| Contact us tcutaiwan@gmail.com No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan |