Team:INSA-Lyon/molecular

From 2014.igem.org

(Difference between revisions)

Revision as of 13:46, 11 October 2014

Curly'on - IGEM 2014 INSA-LYON

MOLECULAR MODELISATION

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.

@@ Line 16: / Line 16: @@
 		<div id="presentation">
-                        <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>
-<h6 align="left">Methods</h6>
+                        <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>
+<h6 align="left">Methods</h6>
+<p><div align = "justify">
 			<h5 align="left">CsgA Engineering</h5>