Difference between revisions of "Team:Aix-Marseille/Modeling"

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A trun-helix contains 3.6 residues and measures 5.4 Angstrom (1.5 Angstrom per residue).</li>
 
A trun-helix contains 3.6 residues and measures 5.4 Angstrom (1.5 Angstrom per residue).</li>
 
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Revision as of 06:38, 17 September 2015

Chew fight

Our idea

We are delighted to present our models and hope that they will seem clear and explicit. During our project, we have expressed several enzymes and built several systems. Therefore, we needed enzymatic models and computer simulation to assess their effectiveness, their stability, and improved them. We initially chose 3 laccases (B.subtilis, E.coli, T.thermophilus) and 3 cytochromes C (Shewanella oneidensis, Synechocystis sp, Paracoccus denitrificans). The purpose of our simulations was to determine a custom linker for each of our constructions. The challenge was to increase the chances of contact between the two enzymes to allow electron transfer. So we had to simulate a system in which our enzymes are pre-positioned. It also involved the selection of a structured linker (alpha helix) to maintain proper conformation. Another advantage of a linker is a practical one. In fact, it is easier to manipulate one molecule than two. Then, there is no need to observe a proportion ratio.