1. Lex Parsimoniae

    01:28

    from William DeWitt / Added

    25 Plays / / 0 Comments

    Iterating toward a maximum entropy image of the functional heterogeneity of myoglobin. Infrared spectroscopy of a set of myoglobin proteins binding ligand at cryogenic temperatures gives the image on the left. An unknown distribution of protein function across this set determines the data we observe. Modeling the connection from this distribution to the data, we are left with an inverse problem: we have measured the effect, but what was the cause? In the image on the right, this experimental data is transformed to reveal the underlying image of functional and spectral heterogeneity in the ensemble of myoglobin molecules, with unexpected features. These features help us determine which atoms in the protein are modulating its oxygen-binding function. The maximum entropy method (MEM), in the spirit of Occam's razor, steps toward an explanation of the data that is as simple as possible, but no simpler. As we step toward better reconstructions of the data on the left, the simplest possible explanation emerges on the right. Press: uvm.edu/~uvmpr/?Page=News&storyID=17075 The paper in Physical Review Letters: prl.aps.org/abstract/PRL/v105/i9/e098101 This is based on my MS thesis work with Kelvin Chu in the University of Vermont Physics Department. I'm currently a senior scientist at Adaptive Biotechnologies in Seattle, working on computational genomics of the Adaptive immune repertoire. I also work as an ambassador for Imagine Science Films: imaginesciencefilms.org Music: hydroscope by Gallery Six (http://soundcloud.com/gallery-six)

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