Turning data into sound to discover the incredible speed & complexity of the proteins in our brains
When I was first diagnosed with RBD (REM-Sleep Behavior Disorder) and Hyposmia, I was told it was because of a mis-folding protein in my brain.
Later tests turned up evidence of this protein, folded into a seemingly abnormal and toxic form.
With it comes a high risk of developing a more serious neurodegenerative condition.
Alpha-synuclein is the protein in question here, and is most often associated with Parkinson’s Disease, much the way that Beta-amyloid is seen in Alzheimer’s.
While these proteins have been portrayed (perhaps over-simplistically) as the bad guys, there is now debate on what may be cause and what may be an effect. However, it is still true that these mis-folded proteins do often correlate with neurodegenerative problems.
But what do we mean when we think of a protein “mis-folding”?
A new study, that made use of the skills of a musical composer, has shed light on just how complex and lightning fast, this process is.
Martin Gruebele, a Chemistry Professor at University of Illinois Urbana-Champaign, worked with composer and software developer Carla Scaletti to come up with a new way to observe the process, using “data sonification” as a way to turn their data on each step of a folding protein into sound.
This new approach has revealed a couple of amazing facts:
1. Not only are there tens of thousands of interactions between a protein’s hydrogen bonds and the surrounding water molecules that take place between the unfolded and the unfolded state, but
2. The process takes place during an incredibly short window (between seventy nanoseconds and two microseconds) in time.
The report on the full study details and their approach can be seen here:
For me this deeper understanding strips away some of the simplistic thinking about particular proteins as good or bad, and points both to how much we still have to learn, and also to the incredible majesty and diversity of our biology.
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