The romantic twist of beta sheets

Thomas Cole's Romantic Landscape with Ruined Tower

So I am going further and further into the genomics rabbit hole and I am loving what I am finding! The genetics I remember encountering in undergrad was so dry, so static, so...lacking in dynamism!
How does one compete with the image of an Ecologist, that adventurous, jungle/island/mountain/tundra/desert/reef/volcano/ocean-bound Earth trekker? Any bench-bound Molecular Biologist pipetting fluids from one tube into another tube would seem rather tame, right? I certainly thought so.
But little by little, the more I scratched at the surface the more wonders and curiosities I uncovered. And now, years later (eons it feels like!), I am discovering how completely wrong I was. Somewhere in between learning about the mysterious structure of chromatin and reading about the puzzling habits of enhancers...I think I fell in love.
This world is moodier and more chaotic than a westbound journey 'round Cape Horn!

But I digress. The reason I even thought to post tonight was because I uncovered a delightful bit of protein trivia:
So first off you need to understand that the ability for a protein to function depends on how they fold. There are many different levels of folding which I will not get into too much now, but know that this folding ultimately occurs due to the sequence of amino acids that make up that protein*. As you would imagine, there are tons and tons of proteins that perform diverse activities (some recognizable ones: hemoglobin, insulin, collagen, etc). You would think that there must be a seemingly infinite number of ways to fold a protein in order for it to carry out its specific task - and you are right...but fear not, for there is order in the madness! Those complicated bunches of amino acids can actually be divvied up into many smaller, recognizable structures called structural motifs. Some structural motifs are more common than others and thus can be seen in many different kinds of proteins. One of these is called a Greek key motif:

A snapshot of a segment of amino acids in this protein show us there are 4 connecting beta sheets**. This looping pattern is reminiscent of the common Greek design, the Greek key and is thus aptly named:

Added Oct 12, 2012

This was described and named by Dr. Jane S. Richardson*** who has been a pioneer in the field of protein structure since the 1970s. Lovely, eh? I have to wait til I get on the school network to download the paper but I can't wait to read it! I love finding things like this in science, especially in a field that is not known for quirks. Things like this are just so delightful to find. Obviously this is a reflection on how much I love etymology and taxonomy, there are always so many hidden relationships in words and names. Maybe one day I will discover something and get to name it after some semi-obscure thing students in the future will be compelled to look up and spend over an hour researching!






*So proteins all start of with their DNA sequence which gets transcribed into RNA, spliced [edited] into mRNA, which then feeds into a ribosome that then translates that string of nucleotide bases into a string of amino acids which then scrunch up and twist and fold according to how they came out!

** beta sheets are flat configurations (contrast that to the alpha helix structure)

*** Remember seeing all those 3-D ribbon images of proteins from your textbooks? Well, you can thank Dr. Richardson for those! She created those ribbon diagrams that are now ubiquitous in science textbooks:

Triose phosphate isomerase hand-drawn by Jane Richardson in 1981

Richardson, J. S. 1977. B-sheet topology and the relatedness of proteins. Nature 268: 495-500.