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gfp structure
gfp structure
The green fluoresent protein GFP was made by the jellyfish Aequorea victoria. Jellyfish are generally translucent, but frequently decorated by brightly luminescent structures. In 1991 Prasher et al. Cloned the gene of GFP and the crystal structure of GFP was solved in 1996.
Sialobiology: Structure, Biosynthesis and Function. Sialic Acid Google Livres.
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Green fluorescent protein: structure, folding and chromophore maturation. PubMed NCBI.
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Fluorescent Proteins From the Beginnings to the Nobel Prize Learn Share Leica Microsystems.
Because of its enhancements this GFP variant was called enhanced GFP or EGFP. By doing structural research on GFP Tsien and coworkers developed further fluorescent derivates. With the GFP structure in their hands they established a variant T203Y which was shining in bright yellow and was therefore given the name yellow" fluorescent protein" or YFP.
Finally, the chromophore maturation half-life is close to 30 minutes, which limits the use of wt-GFP as a reporter for rapid gene inductions 4, 5. To address the limitations of wt-GFP, molecular biologists created the wt-GFP variant called enhanced green fluorescent protein PDB: 4EUL, or EGFP, which contains the mutations Phe-64-Leu and Ser-65-Thr 3. EGFP has a molecular weight of 26897.43, Da and a pI of 5.58 2. EGFP exists as a monomer and also has the same secondary structures as wt-GFP because the mutations occur within the core 3 10 helix and chromophore and do not affect overall protein structure.
Biological Assembly 1. Structure Factors CIF. Structure Factors CIF gz. Validation Full PDF. fo-fc Map DSN6. 2fo-fc Map DSN6. Map Coefficients MTZ format. CRYSTAL STRUCTURE OF THE GREEN FLUORESCENT PROTEIN GFP VARIANT YFP-H148Q WITH TWO BOUND IODIDES. Classificationnbsp: LUMINESCENT PROTEIN.
GFP-tagging in Fluorescence Microscopy.
The GFP that was first isolated from the jellyfish, Aequorea victoria, is known as wild-type or wtGFP and is the most widely used GFP. The structure of GFP includes the primary structure of a chain of 238 amino acids, and a secondary structure of hydrogen-bonded helices and pleated sheets and a tertiary barrel shaped structure capped with helices.
GFP imaging: methodology and application to investigate cellular compartmentation in plants Journal of Experimental Botany Oxford Academic.
Observations of changes in positions and movement of compartments can be made by labelling them with fluorescent probes whose signals can be distinguished from one another. A few plant compartments and structures are naturally autofluorescent at wavelengths distinct from GFP excitation and emission, allowing visualization of a GFPlabelled structure along with the autofluorescent body.
Green Fluorescent Protein The Embryo Project Encyclopedia. Green Fluorescent Protein.
Shimomura focused on aequorin, purified the protein, crystallized it, and elucidated its underlying structure. He also studied the properties of GFP, and published his last paper on GFP in 1979. In 1981, after leaving Princeton University for the Marine Biology Laboratory in Woods Hole, Massachusetts, Shimomura did not research on GFP anymore. From 1979 to 1992, many researchers studied various aspects of GFP, including the use of Nuclear Magnetic Resonance to study the amino acids of the protein, the use of X-rays to study its crystal, and the evolution of GFP. In the early 1990s, molecular biologist Douglas Prasher, at the Marine Biology Laboratory, used GFP to design probes, a technology involving fragments of DNA to detect the presence of nucleotide sequences. Prasher isolated the complementary DNA cDNA of Gfp gene, and he published the sequence of the gene in 1992.

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