Featured image: a 3D illustration of an enzyme. Since enzymes have a rich structure like the molecule in this image, they are tuned to perform specific reactions inside the body. (From Argonne National Laboratory).
This week, we invited Christin Monroe, a fifth-year graduate student in the Department of Chemistry at Princeton University, to come in and speak with us about enzyme production. Christin uses a variety of organisms, from E. coli to yeast, as factories for enzymes–3D molecules that perform specific chemical reactions, like hemoglobin carrying oxygen through your veins.
As a student in Professor Grove’s group, Christin first teaches a colony of bacteria to produce the enzyme in question. Basically, this involves getting a strand of DNA from an organism that produces an enzyme naturally, and stuffing this inside the creatures in a Petri dish (of course, it’s harder than it sounds!). Then, if the host understands its genetic instructions, it mass-produces the enzyme so that Christin can harvest it and purify it enough for further analysis.
That next step could involve all sorts of applications. Maybe the isolated enzyme is critical for a certain medicine to work in the human body, so its reactions with a particular drug are analyzed to minimize side effects. Or, the enzyme could digest some contaminants in our drinking water (as tested in Belgium), cleaning it for us and then decaying away. After all, enzymes are naturally biodegradable, so they perform much better and cleaner than the synthetic alternatives that chemists might produce inorganically.
Sometimes, the reaction between and enzyme and another chemical happens in stages, and these intermediate byproducts are crucial to understand. Maybe they cause unintended side-effects from drugs, or maybe they signify other chemical uses for the enzyme aside from the obvious. In any case, researchers need to look inside the quick reaction: so they might “freeze” the reactions to view these byproducts. Or, they might keep a careful eye on the reaction’s progress with diagnostics like spectroscopy, which watches the color of light emitted from a chemical to identify its changes in time.
Christin is more than a chemist–she has also organized several outreach programs here at Princeton. One of them, a series of lectures and career-services mentoring events throughout August 2016, is happening in partnership with the American Chemical Society, and will feature a public talk by Bassam Shakhashiri. Check it out: there’s more information on this page’s second story.
After the interview, Brian and Stevie moved on to the very serious topic of Arctic ice melting, which is so concrete that a cruise liner will be able to pass through the Arctic Ocean this August. This has never been possible for such a big ship before, so it goes toshow how quickly our ice caps are disintegrating (and allowing for morally questionable commercial ventures to jump in and take advantage of the new open seas). Afterwards, we discussed the not-so-serious naming of the new British Antarctic Survey ship, which will take on the name (thanks to the Internet) Boaty McBoatface.
Lastly, we ask a broad question: should science be done for application’s sake, or for nothing but curiosity? Most science questions originate when a researcher finds something interesting and wants to find out more, but generally they get funded when the researcher connects the question to an application in engineering that might benefit society. But research for its own sake can produce spin-off technologies that were never expected, and also provides the chance for revolutionary results instead of incremental progress. Plus, humans are curious: shouldn’t we satisfy the urge to know more, especially if it leads to scientific truths unbiased by the economic forces around us?
As always, you can find the playlist for the show on WPRB.com, or below.