Abstract
Light is produced from several bioluminescent species through the action of green fluorescent proteins (GFPs) (reviewed in ref. 1). One such GFP from the jellyfish Aequorea victoria fluoresces following the transfer of energy from the Ca2+-activated photoprotein aequorin(2,3). This energy transfer mechanism is radiationless, and proceeds via the interaction of these two proteins in photogenic cells located at the base of the jellyfish. Expression of GFP in vivo does not alter the spectral properties of the protein (4). Full-length GFP appears to be required for fluorescence, however the chromophore responsible for light absorption is located within a hexapeptide at positions 64–69 (5). This region of GFP contains a Ser65-dehydro Tyr66-Gly67 cyclic tripeptide which functions as the minimal chromophore.
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Kain, S.R., Kitts, P. (1997). Expression and Detection of Green Fluorescent Protein (GFP). In: Tuan, R.S. (eds) Recombinant Protein Protocols. Methods in Molecular Biology™, vol 63. Humana Press. https://doi.org/10.1385/0-89603-481-X:305
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DOI: https://doi.org/10.1385/0-89603-481-X:305
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