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Fluorescent Protein Research Lands Scientists Nobel Prize

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."

2 of 79 comments (clear)

  1. Re:Good for them! by Anonymous Coward · · 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).

  2. Re:Good for them! by Hatta · · 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.

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