- GFP consist of 238 amino acids and this chain folds up into the shape of an aluminum beverage can. Inside the can-like structure, amino acids 65, 66, 67 form the chemical group that absorbs UV and blue light, and fluoresces green. (Credit: Image courtesy of Nobel Foundation)
The 2008 Nobel Prize in Chemistry was jointly awarded to Osamu Shimomura (Marine Biological Laboratory and Boston University Medical School), Martin Chalfie (Columbia University), and Roger Y. Tsien (University of California, San Diego). Green fluorescent protein (GFP) was first observed in the jellyfish Aequorea victoria in 1962. Further important developments led to the use of GFP as a tagging tool which, once bound to a protein of interest, can permit detailed studies of a number of biological interactions.
Shimomura first isolated the protein and discovered that it glowed bright green under ultraviolet light. Chalfie demonstrated that GFP was valuable as a luminous genetic tag in his early studies of GFP in Caenorhabditis elegans. Tsien studied how GFP fluoresces and extended the color palette to give various proteins and cells different colors.
(Excerpts from ScienceDaily, October 8, 2008)
