- Carnegie Mellon UniversityPhD Student, 2013 - present
- KAISTVisitin Scholar, 2012 - 2013
- Adaptive EquipmentDesigner, 2011 - 2012
- Freelance ConsultingInnovation Strategy and Design Consulting, 2004 - 2008
- Carnegie Mellon UniversityPhD - Mechanical Engineering, 2013 - present
- KAISTMS - Industrial Design, 2009 - 2010Studied user creativity as a driving force in design
- RMIT UniversityBDes - Industrial Design, 2004 - 2007Studied representations for large scale collaboration and distribution in design work
- Zhejiang UniversityExchange Student - Industrial Design, 2006 - 2006Worked in a design lab and learnt a lot about the industry in China
- University of FloridaNon Degree Student - Mathematics & Innovation, 2001 - 2003Studied math and patent law
- Eastside High School - EHSInternational Bacheloriate, 1999 - 2003Focused on Math, Chemistry and Robotics.
- Marist College Canberra1998 - 1999
Thanks Erin, perhaps this will motivate me to use Google+ more.
I'm doing this course because I'm interested to see where it will take me. In my current work I'm learning new disciplines (synthetic biology and computational systems design) which seem interesting for the application of design and creativity, and I thought this course might keep my mind in a good place on these matters.
Where does this ATP come from? It is synthesized by an incredibly sophisticated molecular machine, the ATP synthase, embedded in the inner membrane of our mitochondria. Energy from the oxidation of food results in protons being pumped across the membrane to create a proton gradient. The protons drive the rotation of a circular ring of proteins in the membrane that in turn move a central shaft. The shaft interacts sequentially with one of 3 catalytic sites within a hexamer, making ATP (little butterflies in the movie!). The ATP synthase rotates about 150 times/second
To visualize the rotation under a microscope, a very long fluorescent rod (actin filament) was chemically attached to the central shaft. Watch real movies (not animations!) of the enzyme spinning here: http://www.k2.phys.waseda.ac.jp/F1movies/F1long.htm
Notice the rotation is slower with longer rods. The rotor produces a torque of 40 pN nm (40 pico Newtons x nanometer), irrespective of the load. This would be the force you would need to rotate a 500 m long rod while standing at the bottom of a large swimming pool at the rate shown in the movie.
How did this amazing rotor evolve? The hexameric structure is related to DNA helicases that rotate along the DNA double helix, using ATP to unzip the two strands apart. The H+ motor has precedence in flagella motors that use proton gradients to drive rotation of long filaments, allowing bacteria to tumble through their surroundings. At some point, a H+ driven motor came together with a helicase like hexamer to create a rotor driving the hexamer in reverse, to synthesize ATP.
The 1997 Nobel prize in Chemistry was awarded to John Walker and Paul Boyer for solving the structure and cyclical mechanism of the ATP synthase, respectively. This amazing enzyme was also the subject of my own Ph.D. thesis, and my first love!
For #ScienceSunday curated by and .
The mailing list they are using to manage the groups seems a little buggy. I noticed it looked like some people were not getting all of the messages.
Hopefully this will be worked out before too long.
Anyway, nice to meet you all.
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