Difference between revisions of "Team:UNSW Australia/Medals"
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Revision as of 13:56, 17 October 2018
Medals
The iGEM competition has many components, all of which are essential. Below is a list of the medal judging criteria, how we have met that criteria, and a link to the pages on which you can find that information. Click on the medals to toggle between the juging criteria.
| Criteria | Description |
|---|---|
| Registration and Attendance | Our team, UNSW Australia is registered, and we have 11 team members and our two PI’s attending the conference. |
| Wiki | You are already here! Use our navigation bar up the top to visit our pages and see all the work we've done this year! |
| Poster | Our poster session is on the Saturday of the Giant Jamboree! |
| Presentation | Our presentation is on the Saturday of the Giant Jamboree! |
| Judging Form | You can find it here. |
| Attributions | We have successfully summarised all of the external help received during this project. See our page here. |
| Interlab Study | We successfully completed the study, and had a great time doing it! More details on how we ran the study can be found on the Interlab page. |
| Criteria | Description |
|---|---|
| Validated Part | We successfully created RFC10 compatible BioBricks linked to our project, sequenced and characterised them experimentally, and sent them off for judging. The BioBricks we are submitting for silver are BBa_K2710000, BBa_K2710001 and BBa_K2710002. |
| Collaboration | We collaborated with five iGEM teams from all around the world. We collaborated with the Macquarie University team by inviting them to present at our symposium and accepting transformed cell lines. We also collaborated with teams from the Pasteur Institute Paris, Zhejiang University, the National Technical University of Athens, and Paris Descartes University. You can read about our collaborations in more detail, here. |
| Human Practices | Our team has thought carefully about the implications that science can have on the broader world, in a variety of creative ways – and with a range of creative outcomes. We have considered the intersection of our project and the law, and how the law impacts both funding and protection of ideas. From this, we have produced a policy submissions guide and submission, in order to prompt further discussion on the correct balance of protection and stimulating innovation in science. We have also considered how our system may translate commercially, and how we can facilitate its use in practical industries like pharmaceutical production. Finally, we taught and presented our project (and synthetic biology) to a variety of people across society, including 120 people at a symposium we ran, students on a high school excursion that we organised for them, in Arts courses, and science academics. This was important because we realised that you cannot do research in a bubble – you need to engage with both the next generation and the people around you who rely on and engage with your inventions. |
| Criteria | Description |
|---|---|
| Model | Our modelling work was used to inform the design of our system, verifying that our choice of a prefoldin scaffold lends itself well to enzyme clustering. Our model is simple to operate and can be altered for different enzymes based on the specific kinetic parameters of an enzyme's reaction. We modelled the effect that distance between enzymes has on final production yields in an enzyme reaction. Our results showed that clustering enzymes improves reaction yield, and thus justified our experimental hypothesis. In designing our model we engaged with industry and academic sources to verify the underlying assumptions and feasibility of validating our model with experimental data. The final model employed the finite element method to solve a numerical solution of Fick’s diffusion equation, with rates of substrate production and consumption at enzymes in the system controlled by Michaelis-Menten kinetics. |
| Integrated Human Practices | Our project's human practices elements have informed the direction of our scaffold design and experimental methodologies. Industry visits and consultations led the team to consider the modularity of the scaffold, and how this was a great advantage. Modelling work was then undertaken to allow us to model different enzymes to assess if they would be commercially viable. Talking to industry also meant that we saw the need for a thermostable and chemically stable scaffold that would self-assemble, so that it would be easy to use and apply in many different contexts, which was implemented with the choice of prefoldin. We also decided on our covalent protein attachment mechanism after human practices research into the legalities of using the mechanism determined that there were no legal issues with using that mechanism in Australia - otherwise another mechanism with more cross-reactivity would have been used. Legal research was also used to confirm that our system was not patentable. |
| Improved BioBrick | We successfully improved an RFC10 compatible BioBrick linked to our project, characterised it experimentally and sent it off for judging. The BioBrick we were improving was BBa_K812020, which was a BioBrick expressing the enzyme IAAH, involved in indole acetic acid synthesis. We improved the part by adding a His tag and a Spy tag. The improved BioBrick number is BBa_K2710005 and more information about how we experimentally validated the improvement can be found on our improve page. |