Nobel season '08: Chemistry

After a very busy day, I'm nerdily cheering in my seat over today's announcement that the Nobel prize for chemistry goes to Osamu Shimomura, Martin Chalfie and Roger Y. Tsien for the discovery and development of the green fluorescent protein, GFP, a protein first isolated from a jellyfish that glows bright neon green when irradiated with UV light.

From the Nobel prize website:

This year's Nobel Prize in Chemistry rewards the initial discovery of GFP and a series of important developments which have led to its use as a tagging tool in bioscience. By using DNA technology, researchers can now connect GFP to other interesting, but otherwise invisible, proteins. This glowing marker allows them to watch the movements, positions and interactions of the tagged proteins.

There are few words that could overstate the significance of this technique in molecular biology and of the many wonderful findings that it has lead to. The ability to tag a molecular process in such a way that you could follow it through time and space by looking through a microscope while it happens (!!!) is nothing short of a revolution. There is a definite before and after. A member of the academy just described it on the news as the difference between watching all of a Shakespearean play and arriving at the end when everyone is dead to try to figure out what had happened. We can study individual proteins in individual living cells, identify in which cells a particular protein is produced, when it's produced, under what conditions it's produced, where in the cell it goes and if it interacts with other proteins. We can follow how genes are expressed, how the DNA molecule is structured into chromosomes, how chromosomes replicate, how cells divide, how different cells develop... I can go on.

GFP is a green glowing protein, but since its discovery we've gotten blue fluorescent, protein, cyan fluorescent protein, yellow fluorescent protein; fluorescent proteins with such tasty names as mPlum, mGrape, mRaspberry, mStrawberry, mCherry, mTangerine, mBanana, mHoneydew; fluorescent proteins that change color depending on pH; and now it's possible to colour cells in pretty much any shade you'd want.

GFP was first identified in the beautiful bioluminescent jellyfish Aequorea victoria. This is relevant for a couple of reasons. First of all, look what can come out of basic science when you're not even trying! I doubt Osamu Shimomura had a Nobel prize in mind when he was squeezing jellyfish into pulp to try to find out what it was that made them glow. Right? Secondly, the reason we are able to take a protein that's normally produced in a jellyfish, put it in a human cell, in bacteria or in a worm and make it work is due to the fact that we all share a common ancestry! In the perspective of it all this is just a small side thought, but that doesn't make it any less beautiful. Lastly, now that we are peeking into the "post-genomic era" we have the possibility of identifying interesting genes directly when we see a critter do something cool. Who knows what other interesting things are lurking in genomes out there, just waiting for us to learn more about them and possibly find a useful application for them.

I'm very happy with the choice of laureates this year, especially with the chemistry prize's emphasis on biology, and it's going to be really interesting to hear what the laureates have to say when they come around to Uppsala in December.

Swedish blog tags: Vetenskap, Biologi, Nobel, Nobelpris
Technorati tags: Science, Biology, Nobel prize, Chemistry, GFP