[3], Protein Database (PDBsum): 3omv. European Bioinformatics (EBI); 2009.</ref> GFP converts the blue chemiluminescent of aequorin in the jellyfish into green fluorescent light.[1] It remains unclear why these jellyfish use fluorescence, why green is better than blue, or why they produce a separate protein for green fluorescence as opposed to simply mutating the present aequorin to shift its wavelength,[2] but in the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, interactions between various membrane and cytoplasmic proteins, as well as many others.[3]
References
- ↑ [1], Yang F, Moss LG, Phillips GN Jr. 1996. The molecular structure of green fluorescent protein. Biotechnology. 14: 1246-1251. DOI 10.1038/nbt1096-1246.
- ↑ Cite error: Invalid
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- ↑ [2], Haldar S, Chattopadhyay A. 2009. The green journey. J Fluoresc. 19:1-2. DOI 10.1007/s10895-008-0455-6; biographical background on Douglas Prasher, Martin Chalfie and Roger Tsien.
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