Team:INSA-Lyon/molecular
From 2014.igem.org
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- | + | <p><div align = "justify"> One of the main goals of our modeling work this year was to understand the <b>structure</b> of the curlin subunit protein, <b>CsgA</b> and it's behavior when engineered with a tag constituted of either six histidines (that we will call <b>His1-tag</b> from now on) or twice that motif (<b>His2-tag</b>), since such a peptide is known for its nickel chelation properties.<br\> | |
- | + | We then discussed over our results with the wetlab members to define a way to confirm the accuracy of our model, and so we were able to assess that, in accordance with litterature, the <b>best position</b> for the tag was by the <b>C-terminus</b> of the protein. We also determined that the His-tag was likely to take <b>floating conformation</b> instead of folding itself around CsgA. </div></p> | |
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- | < | + | <h6 align="left">Methods</h6> |
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- | < | + | <h5 align="left">CsgA Engineering</h5> |
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Revision as of 13:44, 11 October 2014
One of the main goals of our modeling work this year was to understand the structure of the curlin subunit protein, CsgA and it's behavior when engineered with a tag constituted of either six histidines (that we will call His1-tag from now on) or twice that motif (His2-tag), since such a peptide is known for its nickel chelation properties.
We then discussed over our results with the wetlab members to define a way to confirm the accuracy of our model, and so we were able to assess that, in accordance with litterature, the best position for the tag was by the C-terminus of the protein. We also determined that the His-tag was likely to take floating conformation instead of folding itself around CsgA.
We then discussed over our results with the wetlab members to define a way to confirm the accuracy of our model, and so we were able to assess that, in accordance with litterature, the best position for the tag was by the C-terminus of the protein. We also determined that the His-tag was likely to take floating conformation instead of folding itself around CsgA.