Green Fluorescent Protein

Title: Green Fluorescent Protein
Additional Names: GFP
Literature References: Class of autofluorescent proteins found in bioluminescent coelenterates where they function as energy transfer acceptors, emitting a green fluorescent light (lmax = 509 nm). Acidic globular proteins consisting of 238 amino acids, monomeric mol wt ~30,000. Developed commercially as a biochemical tool to visualize cellular structure and monitor dynamic cellular events via fluorescence resonance energy transfer (FRET) assays. Purifn, characterization and energry transfer studies from Aequorea victoria: H. Morise et al., Biochemistry 13, 2656 (1974); from Renilla reniformis: W. W. Ward, M. J. Cormier, J. Biol. Chem. 254, 781 (1979). Properties of naturally occurring proteins: M. Chalfie, Photochem. Photobiol. 62, 651 (1995). Structural studies of chromophore fragment: G. N. Phillips, Jr., Curr. Opin. Struct. Biol. 7, 821 (1997); B. R. Branchini et al., J. Am. Chem. Soc. 120, 1 (1998). Fluorescence and spectral properties of variants genetically engineered for enhanced fluorescence: G. H. Patterson et al., Biophys. J. 73, 2782 (1997); R. H. Stauber et al., BioTechniques 24, 462 (1998); for Ca2+ visualization: T. Nagai et al., Proc. Natl. Acad. Sci. USA 98, 3197 (2001). Review of expression and detection: S. R. Kain, P. Kitts, Methods Mol. Biol. 63, 305-324 (1997). Review of research applications: T. Misteli, D. L. Spector, Nat. Biotechnol. 15, 961-964 (1997); as reporter gene: S. R. Kain et al., BioTechniques 19, 650-655 (1995); as fluorescent protein tag: H.-H. Gerdes, C. Kaether, FEBS Lett. 389, 44-47 (1996). Bibliography: L. J. Kricka, P. E. Stanley, J. Biolumin. Chemilumin. 12, 113-134 (1997).
Use: Research tool in cell biology.
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Green fluorescent protein
PDB 1ema EBI.jpg
Structure of the Aequorea victoria green fluorescent protein.[1]
Symbol GFP
Pfam PF01353
Pfam clan CL0069
InterPro IPR011584
SCOP 1ema

The green fluorescent protein (GFP) is a protein composed of 238 amino acid residues (26.9 kDa) that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range.[2][3] Although many other marine organisms have similar green fluorescent proteins, GFP traditionally refers to the protein first isolated from the jellyfish Aequorea victoria. The GFP from A. victoria has a major excitation peak at a wavelength of 395 nm and a minor one at 475 nm. Its emission peak is at 509 nm, which is in the lower green portion of the visible spectrum. The fluorescence quantum yield (QY) of GFP is 0.79. The GFP from the sea pansy (Renilla reniformis) has a single major excitation peak at 498 nm.

In cell and molecular biology, the GFP gene is frequently used as a reporter of expression.[4] In modified forms it has been used to make biosensors, and many animals have been created that express GFP as a proof-of-concept that a gene can be expressed throughout a given organism. The GFP gene can be introduced into organisms and maintained in their genome through breeding, injection with a viral vector, or cell transformation. To date, the GFP gene has been introduced and expressed in many Bacteria, Yeast and other Fungi, fish (such as zebrafish), plant, fly, and mammalian cells, including human. Martin Chalfie, Osamu Shimomura, and Roger Y. Tsien were awarded the 2008 Nobel Prize in Chemistry on 10 October 2008 for their discovery and development of the green fluorescent protein.