1 post tagged “protein folding”

So, when I was a young scientist, I didn’t work on drug targets or diseases or anything remotely seen as practical.  I worked in a fairly esoteric field – protein folding and protein stability.   Why?  Well, because I thought it was cool.  No, really.

Anyway, everyone outside of certain parts of Kansas and Louisiana knows that DNA is the genetic material that makes us what we are.  However, DNA is BORING.  It sits in the nucleus under essentially cellular lock and key.  How come?  Well, mostly because it’s so important that you don’t want it out in the cellular milieu because it could get damaged.  And in the good-bad scheme of things, that’s bad.  So, DNA does what any good manager does, it delegates.   And it delegates nearly all the cell’s to-do list to proteins.

Proteins are long chains of amino acids that fold into three-dimensional structures in the cell.  This structure dictates what they “do”: whether it’s be an enzyme, a receptor, a structural component, a messenger, and so forth.  In the 1970s, it was shown that proteins could reversibly fold and unfold – but the “whys” and “hows” of that were still a mystery.

So – I worked on some of that.  Why some proteins folded more readily than others and what made some more stable than others (those two were not always correlated).  But what was it good for my wise mother would ask me?  And I’d tell her,  “Errrr, well Mom, it helps our understanding of biophysics and blah blah woof woof…” until her eyes glazed over.  Later, I became disenchanted with the “academic” aspect of protein folding studies and moved onto real-world drug discovery and got into anti-infectives and endocrinology.

Guess what?  As it turns out over the next decade or so protein folding (or mistakes in it) have been implicated mechanistically in several diseases – including Alzheimer’s Disease, cystic fibrosis, mad-cow like diseases and even some cancers.

Today, I came across a paper in which scientists in San Antonio examined differences in the behavior in proteins between mice and bats.  Why mice and bats?  Well – no offense to pigeons – bats are essentially rats-with-wings and genetically very similar.  One difference is that bats live a lot longer than mice.

As it turns out, proteins from bats are more resistant to oxidative damage than their murine counterparts (oxidation is linked to age-dependent damage and disease) and their protein folds are more stable, too.  

Go figure.  Rather than blather on to my mom about biochemistry and biophysics, I could have told her I was working on the Holy Grail of biology: Longevity.  In essence, the Fountain of Youth!

Oh – and guess where the bats from that study live?  Florida.