Refolding of Proteins to their Native State

So I spent a solid two hours just trying to get reliable sources on this article I saw on the internet where researchers supposedly “unboiled” an egg (http://www.cnbc.com/id/102364302). I happened upon that article a few days ago when my Orgo chem classmate shared it on Facebook. My initial reaction was that of amazement. One of the first things you learn in basic biochemistry is that it’s extremely difficult to renature a protein once it has denatured. The free energy landscape consists of numerous energy minimas where a protein can get trapped in when it attempts to refold properly. Armed with this knowledge, my excitement slowly died down to skepticism. CNBC is a reliable news network but it often happens that journalists misrepresent recent discoveries in Science. I had to understand what was going on.

This article gnawed at me ever since I read it because the headline sounds too good to be true. So I tried reading on the vortex fluidic device (VFD), the machine that was used in the experiment. However, it’s an extremely difficult read unless you’re a Chemist or an Engineer. One of my frustrations as a biology major is that I’m not equipped with the technical knowledge to understand complex machines. I supposedly have “biotechnology” in my degree as well but I think I only have superficial knowledge to actually merit that title in my diploma when I graduate. I once attempted to read a paper on a continuous process for producing biofuels from algae a few years ago and I can’t even say I understood 25% of what the authors wrote. There was simply too many references to unit operations and chromatography techniques that I have no prior knowledge on. I downloaded that paper and hoped that someday I will be able to understand what the researchers did.

Going back to the article I read, the VFD is essentially a machine that spins liquid into a very thin film in order to speed up a chemical reaction. You get a similar vortex when you mix powdered drinks like Tang in a glass of water. It’s just that this process is more controlled. I eventually found a freely available preview page from the original paper published. It included Weiss, who co-authored the first Chemical Biology textbook as my batchmate, Mao, pointed out (I won’t digress again from the discussion. I’ll probably just make another entry about my fascination with Chemical Biology in the future)  Being a preview page I only got a glimpse of the paper but I think this summarizes what they did:

“We imagined applying the VFD with a similar range of input energies to the refolding of proteins…”

Since the folding of a protein to its native state is just a thermodynamic process, I think they just made the the folding more favorable. However, I’m really disappointed because I can’t get into the details because the paper is behind a paywall. While I understand that publishers need to get money from papers, I hope that my university can provide us with subscriptions to these publications. We are a state university after all

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