Fluorescent Protein Research Lands Scientists Nobel Prize 79
Iddo Genuth writes "The Royal Swedish Academy of Sciences has announced three recipients of the Nobel Prize in Chemistry award for 2008: jointly given to Osamu Shimomura, Martin Chalfie and Roger Y. Tsien 'for the discovery and development of the green fluorescent protein, GFP' — a remarkable brightly glowing green fluorescent protein first observed in the beautiful jellyfish, Aequorea victoria, in 1962."
Re:Good for them! (Score:2, Informative)
The remarkable brightly glowing green fluorescent protein, GFP, was first observed in the beautiful jellyfish, Aequorea victoria in 1962. Since then, this protein has become one of the most important tools used in contemporary bioscience. With the aid of GFP, researchers have developed ways to watch processes that were previously invisible, such as the development of nerve cells in the brain or how cancer cells spread.
Tens of thousands of different proteins reside in a living organism, controlling important chemical processes in minute detail. If this protein machinery malfunctions, illness and disease often follow. That is why it has been imperative for bioscience to map the role of different proteins in the body.
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.
Researchers can also follow the fate of various cells with the help of GFP: nerve cell damage during Alzheimer's disease or how insulin-producing beta cells are created in the pancreas of a growing embryo. In one spectacular experiment, researchers succeeded in tagging different nerve cells in the brain of a mouse with a kaleidoscope of colours.
Re:Green Eggs and Ham (Score:4, Informative)
Re:Good for them! (Score:5, Informative)
GFP is without a doubt the most commonly used fluorescent tag. It's the workhorse of biological fluorescence microscopy. Given the tens of thousands of publications that have used it, the Nobel prize is certainly deserved.
One of the great things about GFP is that it is a protein. So you can engineer an organism to express GFP. In fact you can engineer the fluorescent protein to be bound to whatever protein you want, just by splicing it into the correct place in the genome. So you can basically make any protein glow. So you can track proteins implicated in cell mobility, or vision, or signaling, or cancer, or some other disease, or whatever.
With modern fluorescent microscopes, you can actually imagine GFP at the single-molecule level. So you can build movies where quite literally you can track individual protein molecules as they move inside a cell. This obviously gives a whole new insight into cellular machinery, and hence everything based on cells (e.g. life and death).
Re:Good for them! (Score:5, Informative)
It sounds silly, but this is one of the great success stories of pure research. GFP has proved to be an absolutely astounding tool for biologists, one that we'd never have if there weren't people curious enough to ask "why does that jellyfish glow?" and people willing to fund them.
I'll cite just one example of this protein being used in a completely novel and extremely powerful way. Fluorescent proteins absorb at one wavelength and emit at another longer wavelength. They've fiddled with the GFP sequence to make yellow and red versions that have overlapping spectra. So now you can tag any two proteins of interest in a cell with GFP and YFP. Next you expose them to light that excites GFP. If the two proteins of interest are closely associated there will be an efficient transfer of energy, and you'll see lots of yellow light emitted. If the proteins of interest are not associated, you'll get mostly green light.
That's right, you can measure the average distance between two proteins with nothing more than 2 fluorescent proteins, a laser and a spectrophotometer. Not only that, but you can do it in a living cell culture, apply pharmaceuticals to the cells and track the change in real time. That's just one of the more amazing uses of GFP, and a great example of why it's so important to fund research with no obvious practical value.
Re:Green Eggs and Ham (Score:3, Informative)
I wouldn't go quite that far, at least not yet. Looking at the last ten Chemistry Nobels, it's about 50-50 between molecular biology and the rest of chemistry. Last year's prize went for work in surface catalysis, 2005 went to the olefin metathesis guys, 2001 was for chiral syntheses, 2000 was for conductive polymers, 1999 was for femtosecond kinetics, and 1998 was for quantum chemistry.
I'll grant that chemistry doesn't have the big questions to solve like physics does, but there are still substantial discoveries out there to be made. Synthesis and catalysis can always be improved, as can analytical techniques. There's been a big push in modern chemistry to make industrial chemistry more enviromentally friendly, which I'm sure will lead to at least one prize specifically for this.
Re:Green Eggs and Ham (Score:1, Informative)
Relatively trivial? Tsien's work on expanding the spectra at which fluorescent proteins emit has been anything but. He and his lab pretty much figured out the chemistry by which normally non-fluorescent amino acids are modified post-translationally (after the protein has been made inside the cell) to create a chain of conjugated Pi electrons (ie several double bonds one after the other). This had never been seen in other proteins. Then he took the backbone of the protein and modified the amino acid sequence to emit at different wavelengths (by changing the composition of the Pi electron chain). This was neither obvious nor trivial, given that even single amino acid changes to a protein can completely destabilize it (and Tsien has created at least 10 variants with fluorescent ranges of over 400nm; from blue all the way to deep red).
Even taking away the immense benefit that this 'tool' has had on molecular biology, the work done to understand the nature by which GFP (and other naturally occuring fluorescent proteins that have been discovered since then) is created and how it works is still immensely useful to organic chemistry and molecular biology.