Fluorescent Proteins Part 2: Genetic Manipulations

This is the second post of a three-part series on fluorescent proteins and neurobiology. The first part is on Osamu Shimomura and the third will be on... the Brainbow! I really can't wait to get to the brainbow. 

So, our good friend Osamu Shimomura discovered green fluorescent protein in a tiny jellyfish. Cool, right? But what the hell can they do with this?

In 1962, not much. When genetic engineer techniques evolved and became viable researched tools in the 1980s, the possibilities became endless many.

The awesome thing with GFP is that you can attach it to other proteins. You just put the gene for it next to the other protein's gene, and when the cell produces the protein, it has a GFP attached to it. It's like magic, only it's real!

Proving the GFP could be attached and expressed by cells was made at Martin Chalfie's lab, the second recipient of the 2008 Nobel prize.

What they do with these proteins is that they attach it to another, then they send light of a particular wavelength on it. It absorbs, and gives back light at a different wavelength. It's not hard to detect that light, and the images we get are better with every passing year.

They modified the GFP to give it a wide range of colours and make it easier to insert. This work was made at Roger Tsien's laboratory. Tsien is the third recipient of the 2008 Nobel prize. He created mutants that were stable and produced a lot of fluorescence.

Pretty colours!

Then he and his lab had fun, put the proteins in bacteria and... created a beach!

That, my friends, is science at its best. Crazy and pretty!