2015 igNobels

The 2015 igNobels are out! Yay Science!

I am indeed a scientist by training and trade though recently my brain has gotten soft and mushy from counting left- and right-handed desks.

Pretty much everyone knows what the Nobel Prize is and the scientists look for the ones in chemistry, physics and medicine just to see what’s hot and whom you might have known back in grad school. But the igNobels are also important because they demonstrate that a lot of real science happens a little bit closer to the ground than the Nobel peaks of that ivory tower. It doesn’t mean that this research is unimportant, it’s that the real world of science isn’t as dry as the Ben Stein monotone and is quite compelling in its own way.

Now I’ve done a lot of silly things to advance my own knowledge of science, such as doing everything (except taking the study medication) that the subjects enrolled into the clinical study I was managing were being asked to do, or drawing 750 mL of my own blood at one go using 15 mL Vacutainers to do a lymphocyte proliferation assay in an attempt to isolate an incredibly faint activation signal by flow cytometry (here’s the publication; if you decide to buy access, that’s me on page 2). I spent way way too much time attempting to develop diagnostic assays to detect potential biomarkers for elucidating progression of neurodegenerative disease, and as a sideline science experiment I am still tinkering with the ideal circulator methodology get a perfectly reliable onsen tamago to eventually generate soft-boiled eggs for ramen.

Have the eyes suddenly rolled into the back of your head?

I bring up self-experimentation and diagnostics because two of the 2015 igNobels went to those fields.

speedbumpOn the diagnostics side, Helen Ashdown and colleagues published a new diagnostic for assessment of appendicitis in the British Medical Journal (reference). They successfully correlated the degree of pain felt by patients as a predictor of acute appendicitis while these patients were driven across speed bumps.

You laugh, but 1) it’s an assessment you can do over the telephone while the patient is en route, and 2) those patients with appendicitis could potentially receive treatment upon arrival all that much quicker. Really sounds like a better use of limited emergency medical resources, doesn’t it?

And on the self-experimentation side, did you know there was something called the Schmidt Sting Pain Index? I didn’t either, but that’s the great part about science because you learn something new every single day. You’ll probably want to avoid bullet ants if you ever read the scale, but Michael L. Smith took the Index one further by using a preset sting level (honey bee; Schmidt Sting Pain Index of 2.0), and mapping out which part of the human physiology those stings might feel most severe (reference). If you are inadvertently stung, you’d prefer to have that at the top of the skull, and no, the most painful area isn’t where you think it might be.

That’s dedication, baby.

I do sincerely salute my fellow scientists for advancing our collective knowledge. And just like your mother telling you to wear clean underpants if you go out just in case of an accident, you never know when this information may come in handy.

And one more thing…

There’s also an igNobel handed out for research on boiled eggs. Or more specifically, how to unfold the proteins of a boiled egg, thereby making the egg runny again (reference). Why would someone want to do that? Dr. Yuan and his team were looking more at protein overexpression systems (that would be recombinant sources), where a bug (bacterium, fungus) is engineered to overexpress a protein that you want to study or produce in an industrial process (e.g. enzymes, insulin, vaccine components). There is a lot of misfolding of the proteins produced in this manner and they form insoluble protein aggregates, which at the very least make things difficult because you have to take those additional steps to untangle the proteins and at the very worst, demonstrate that your process isn’t possible because you generate too much waste and post-processing. You want to do this right and they just happened to decide to use boiled eggs to demonstrate their process possibly because those just happen to be one big mass of tangled proteins aggregates and probably because they were in easy supply. I don’t know and it’s not like I know Dr. Yuan.

Someone in the anti-GMO crowd might come up and say well, you shouldn’t be making recombinant proteins in the first place because you never know what will happen if they escape into the wild (the franken-salmon, the GMO soybean etc).

But think of unfolding the proteins of a boiled egg in this way: the hallmark of a lot of neurodegenerative diseases such as Alzheimer’s Disease, ALS, Parkinson’s Disease and prion diseases (scrapie, Creutzfeld-Jakob Disease, “mad cow”) is abnormal protein accumulation into insoluble protein aggregates. What might be the effect for say, the Alzheimer’s patient population if we managed to use this fundamental research to successfully develop a method to safely untangle Aβ protein aggregates in situ?


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