Difference between revisions of "Team:TCU Taiwan/Modeling/Protein structure"
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| − | <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> |
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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. </br></br> | 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> | ||
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. |
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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. |
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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. |
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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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| Contact us tcutaiwan@gmail.com No.701, Sec. 3, Zhongyang Rd. Hualien 97004, Taiwan |