GFP
Jun 15, 2009 10:28 AM Filed in: Chemistry
Today I watched the 2008 Nobel lectures in chemistry (since they are not available in print). Osamu Shimomura (Nobel lecture; meeting abstract), Roger Tsien (Nobel lecture; meeting abstract) and Martin Chalfie (Nobel lecture; meeting abstract) shared the prize for the discovery and development of green fluorescent protein (GFP).
Osamu Shimomura’s detailed account of the rigors of isolation and crystallization of luciferin were quite interesting. He was then employed to extract luciferin from a jellyfish, only to realize that there was no luciferin present, but instead a protein, aequorin. They sacrificed many jellyfish (2.5 tons, 2000-3000 per day for an entire summer) to acquire enough aequorin to be studied, and it was noted that some small amount of a green light emitting protein was also present (although not in a high enough quantity to be studied). Many years later Shimomura had enough GFP to identify the chromophore.
Roger Tsien’s work builds on Shimomura in that he used site-directed mutagenesis of GFP to change the structure of the chromophore (which is formed by a reaction between fortuitously placed amino acid residues of the protein). Using this methodology he was able to form a host of several differently colored proteins.
Martin Chalfie used GFP technology to study mechanosensation in the nematode C. elegans.
Then in something of a departure, I read about the 2007 Nobel prize in chemistry, given to Gerhard Ertl (Nobel lecture; meeting abstract) who was bestowed the honor for his studies of chemical processes on solid surfaces. He details studies on the Fe-catalyzed conversion of nitrogen into ammonia and the oxidation of CO on Pt surfaces.
Osamu Shimomura’s detailed account of the rigors of isolation and crystallization of luciferin were quite interesting. He was then employed to extract luciferin from a jellyfish, only to realize that there was no luciferin present, but instead a protein, aequorin. They sacrificed many jellyfish (2.5 tons, 2000-3000 per day for an entire summer) to acquire enough aequorin to be studied, and it was noted that some small amount of a green light emitting protein was also present (although not in a high enough quantity to be studied). Many years later Shimomura had enough GFP to identify the chromophore.
Roger Tsien’s work builds on Shimomura in that he used site-directed mutagenesis of GFP to change the structure of the chromophore (which is formed by a reaction between fortuitously placed amino acid residues of the protein). Using this methodology he was able to form a host of several differently colored proteins.
Martin Chalfie used GFP technology to study mechanosensation in the nematode C. elegans.
Then in something of a departure, I read about the 2007 Nobel prize in chemistry, given to Gerhard Ertl (Nobel lecture; meeting abstract) who was bestowed the honor for his studies of chemical processes on solid surfaces. He details studies on the Fe-catalyzed conversion of nitrogen into ammonia and the oxidation of CO on Pt surfaces.