One of my favorite pastimes is reading about situations where experts from different (and seemingly divergent) disciplines get together to discuss interdisciplinary cooperation and mutual progress. All too often scientists segregate themselves according to their area of expertise and only make use of the techniques that they are familiar with or have access to in order to answer the question at hand. While this may be a more comfortable approach to science it tends to overlook the benefits that can be achieved by incorporating techniques from other disciplines into one’s research methodology.
Now for a personal disclosure statement: I am a molecular biologist. I too am guilty of focusing on what I know and ignoring techniques that seem foreign to me. So when I came across a paper that had the term synchotron x-ray fluorescence, my mind froze and I thought that I had accidentally surfed into an area that I was not allowed to enter (but it got through my firewall anyway). My google alert is set to receive articles on protein electrophoresis so I can stay abreast of the latest developments in my field. How did x-ray fluorescence sneak in there? Nonetheless, after overcoming my initial uncertainly, I clicked through to the article which I am glad to report will make an interesting blog post.
In a recent issue of ACS Chemical Biology, Lydia Finney and her team from the Argonne National Laboratory in Argonne, Illinois presented a new use for two relatively old and well-established technologies in the study of protein-metal ion interaction. What I found particularly interesting about this study was its synthesis of analytical techniques common to chemistry and biology. Essentially they ran protein samples on a nondenaturing PAGE, immobilized them on a membrane and performed XRF mapping. While both electroblotting and XRF imaging are common in their respective fields, this is the first time that they have been used in concert to solve a scientific problem. The result is an eloquent technique for analyzing the complex mechanisms that regulate metal toxicity and metalloproteomics.
In a commentary to the article written in the same issue of ACS Chemical Biology, Nathan Zahler notes that the fusion of these techniques opens up the road for several other interesting studies such as assessing the interrelationships in the regulation of different transition metals, the study of post-translational modifications that incorporate non-metallic elements and 2D electrophoretic separations for increased protein resolution and mass spectroscopic identification of metal binding proteins.
Whatever the case may be, this study is a prime example of what can be accomplished by out of the box thinking and networking among like-minded individuals from diverse scientific backgrounds.
How has your research been impacted by incorporating techniques from other disciplines? I’ve heard that there are several scientific societies dedicated to interdisciplinary research. Have you come across groups that are worth investigating?
Finney, L., Chishti, Y., Khare, T., Giometti, C., Levina, A., Lay, P., & Vogt, S. (2010). Imaging Metals in Proteins by Combining Electrophoresis with Rapid X-ray Fluorescence Mapping ACS Chemical Biology, 5 (6), 577-587 DOI: 10.1021/cb1000263