Hectic Spring

Finally I am sitting down to write about my research work this quarter.  Unfortunately I was unexposed to the rays of sunshine in Santa Barbara this spring because all of my time was consumed by studying, research projects, and organizational work with WiSE (Women in Science and Engineering).  My studying mainly involved writing one or two 40 page lab reports a week for an upper division biophysical analytical lab course that included several long in class experiments followed by days of computer programming to fit experimental data with Mathematica and protein amino acids into electron density maps with Coot.  Although I have learned an immense amount from this lab course, including how to create cool three-dimensional pictures of enzymes, the class left me with little spare time to study for other classes.  My research work was also put on the back burner during some weeks when I was scrambling to finish lab reports in the midst of midterms.  However, I continued doing my right angle motif characterization and it will not take me too long to discuss the results I obtained from the first few weeks of the quarter.  I only radioactively labeled two molecules because I wanted to focus on getting good gel electrophoresis results for a few molecules before moving on to other molecules, rather than trying to balance multiple experiments at a time.  Thus the first molecules that I labeled were two different right angle motifs.  I was testing the stability of the right angle structures by their binding strength to a probe molecule.  The more strongly the molecule binds the probe, the less rigid and more floppy the right angle because binding to the probe involves the right angle straightening out (ie, the 90 degree bend changes to a 180 degree line).  Unfortunately, the gel electrophoresis results I obtained were not the best quality; although I could see the titration curve of a probe-right-angle molecule complex forming at high concentrations of the probe and right angle.  Anyways, I am most likely going to have to re-label my molecules with radioactive phosphate and re-do the experiments for better results, but it should be more easy to deal with this summer when I do not have to worry about the hardest class I have ever experienced anymore.  Even though there were several times I thought I was having a severe mental breakdown when a misplaced comma would destroy my entire Matematica program, and I often regretted the amount of time my biochemistry lab class was taking away from me doing research, I am glad that I had the opportunity to go to a school where the biochemistry lab covered such a great extent of material and experimental methods.  I can now say that after three quarters of upper division biochemistry lab I understand a wide range of experimental techniques, from mass spectrometry to x-ray crystallography, to NMR, and how each of the techniques can be applied specifically to biochemistry.  And on top of that I can say that I know how to navigate a number of computational databases for biochemical experimental analysis, and I can definitely handle Mathematica.  So I its a good thing I spent a ton of time studying all the experimental methods employed by biochemists because I never know if any of these techniques may or may not be important to me in my future research, and I have also been introduced to methodologies that I find pretty cool and have sparked my interest in working with them in the future.  That being said I am quite happy that I now have all of that knowledge and can leave the stress of the class behind me.

Posted in 2010-2011, EUREKA

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Alex Iteen is a second year student majoring in Biology. He is interested in bioengineering and synthetic biology. He is currently working in Dr. Fygenson's lab on DNA nanotubes.
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