Team Members:
research team studied and manipulated green fluorescent protein.
Back Ground Information on GFP Protein.
A jellyfish called Aequorea victoria, is what produces the green fluorescent protein. GFP is made out of 238 amino acids and is a very stable protein. The bioluminescent protein (aequorin), found in the jellyfish emits blue light which which is then converted to green light by the green fluorescent protein. This is why the jellyfish glows a fluorescent green. The protein absorbs ultraviolet light from the sunlight, and then emits it at a lower-energy green light. The blue light absorbance is 395nm while the green light is 508nm. The glow comes from a covalently-attached chromophore the intermolecular reaction that happens in the residues ser-tyr-gly. This chromophore is buried deep within the beta barrel, interrupting the helix and keeping it from interacting with the solvent. This fact is what makes GFP so stable. The beta barrel contains 6 alpha helices and 11 beta strands, connected by loops. The loops form a cylinder of beta sheet with anti-parallel strands (also known as the beta barrel).
To View a MDL computer model of GFP visit Jeremy Skramsted and Anneliese Seifert's webpage at:
http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/GFP/template1.html
Or another site at:
http://www-biology.ucsd.edu/~rzeller/GFP/gfproty.html
To view a mutant GFP visit the Protein Data Bank at:
http://www.rcsb.org/pdb/cgi/explore.cgi?pid=174851101177273&page=0&pdbId=1B9C
