Green Fluorescent Protein
From Proteopedia
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Background
Osamu Shimomura, Martin Chalfie and Roger Y. Tsien shared the 2008 Nobel Prize in Chemistry for their for the discovery and development of the green fluorescent protein, GFP.
GFP is small protein (21 kDa) and does not require cofactors to become fluorescent.
Structure
The crystal structure of GFP [1] (Ormö et al., 1996; Yang et al., 1996) is an eleven-stranded anti-parallel beta- barrel, threaded by an alpha-helix, running up along the axis of the cylinder.
The chromophore is in the distorted alpha-helix that runs along the axis of the can, close to the center of the can-like cylinder.
You can take a close look at the of GFP in the PDB entry 1ema.
The chromophore
Additional information on green fluorescent protein
- Roger Y. Tsien (1998) The Green Fluorescent Protein. Annual Review of Biochemistry 67, 509-544.
- [The GFP site] by Marc Zimmer, Ph. D., at Connecticut College, who authored [Glowing Genes: A Revolution In Biotechnology].
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Wayne Decatur, Karsten Theis, Eran Hodis, Laura Carbone, Karl Oberholser, Mark Hoelzer, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky, Joseph M. Steinberger, David Canner
