User:Laura Carbone/Sandbox 1
From Proteopedia
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Green fluorescent protein (GFP) is a bioluminescent polypeptide consisting of 238 residues isolated from the body of [[Aequorea victoria]] jellyfish <ref name="PDBsum">[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&template=main.html], Protein Database (PDBsum): 1ema. European Bioinformatics (EBI); 2009.</ref>. GFP converts the blue chemiluminescent of [[aequorin]] in the jellyfish into green fluorescent light (Yang, Moss, & Phillips, 1996; Phillips, 2007). 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 <ref name="Haldar">[http://www.springerlink.com/content/wvg513864266g77n/fulltext.pdf], Haldar S, Chattopadhyay A. 2009. The green journey. J Fluoresc. 19:1-2. DOI 10.1007/s10895-008-0455-6.</ref>. | Green fluorescent protein (GFP) is a bioluminescent polypeptide consisting of 238 residues isolated from the body of [[Aequorea victoria]] jellyfish <ref name="PDBsum">[http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1ema&template=main.html], Protein Database (PDBsum): 1ema. European Bioinformatics (EBI); 2009.</ref>. GFP converts the blue chemiluminescent of [[aequorin]] in the jellyfish into green fluorescent light (Yang, Moss, & Phillips, 1996; Phillips, 2007). 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 <ref name="Haldar">[http://www.springerlink.com/content/wvg513864266g77n/fulltext.pdf], Haldar S, Chattopadhyay A. 2009. The green journey. J Fluoresc. 19:1-2. DOI 10.1007/s10895-008-0455-6.</ref>. | ||
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| + | Aequorea victoria was first discovered and investigated for its bioluminescence by Frank Johnson, who invited Osamu Shimonmura to work with him in on a small island not far from British Columbia, where the jellyfish is abundant <ref name="Shimonmura">[http://nobelprize.org/nobel_prizes/chemistry/laureates/2008/shimomura_lecture.pdf], Shimonmura O. The discovery of green fluorescent protein. Nobel Prize Lecture; 2009.</ref>. Found off the west coast of the United States between British Columbia and central California (Cowles & Cowles, 2007), the jellyfish was considered a local phenomenon as it would drift in and out of the harbors <ref name="Shimonmura">. | ||
Revision as of 03:02, 2 February 2010
Green fluorescent protein (GFP) is a bioluminescent polypeptide consisting of 238 residues isolated from the body of Aequorea victoria jellyfish [1]. GFP converts the blue chemiluminescent of aequorin in the jellyfish into green fluorescent light (Yang, Moss, & Phillips, 1996; Phillips, 2007). 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 [2].
Aequorea victoria was first discovered and investigated for its bioluminescence by Frank Johnson, who invited Osamu Shimonmura to work with him in on a small island not far from British Columbia, where the jellyfish is abundant [3]. Found off the west coast of the United States between British Columbia and central California (Cowles & Cowles, 2007), the jellyfish was considered a local phenomenon as it would drift in and out of the harbors [3]
