GFP: Green Fluorescent Protein
- "Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer" article by Heim and Tsien tells us that GFP are important for at least three reasons. First, to provide distinguishable markers to observe events going on in a cell simultaneously. Second, to serve as donors and acceptors for fluorescence resonance energy transfer (FRET). Third, to illuminate the structure–function relationship of an intrinsically fascinating protein. Variants of the green fluorescent protein, GFP, with different colors would be very useful for simultaneous comparisons of multiple protein fates, developmental lineages and gene expression levels. Their results demonstrate that the production of more and better GFP variants is possible and worthwhile. The production of such variants facilitates multicolor imaging of differential gene expression, protein localization or cell fate.
http://119.93.223.179/ScienceDirect/Current%20Biology/06-02/sdarticle_022.pdf
- "Crystal structure of the Aequorea victoria Green fluorescent protein" by kormo, cubitt, et al. tells us that the cloning and heterogenous expression of GFP's cDNA were the crucial steps that triggered the widespread and growing use of GFP as a reporter for gene expression and protein localization. GFP is a stable, proteolysis-resistant single chain of 238 residues and has two absorption maxima at about 395 and 475 nm. The relative amplitudes of these two peaks are sensitive to environmental factors and illumination. GFP provides an elegant example of how a visually appealing and useful "function-efficient" fluorescence can be spontaneously generated from a cohesive and economical protein stricture.
http://www.tsienlab.ucsd.edu/Publications/Ormo%201996%20Science%20-
%20Crystal%20structure.PDF
- The article, "Chemical Structure of the Hexapeptide Chromophore of the Aequorea Green-Fluorescent Protein?" by Cody, Prasher, et al. tells us that the GFP proteins are a unique class of proteins involved in the bioluminescence of many cells and organisms. The GFPs serve as energy-transfer acceptors, receiving energy from either a luciferase-oxyluciferin complex or a Ca2+ activated photoprotein, depending on the organism. Upon mechanical stimulation of the organism, GFP emits green light spectrally identical to its fluorescence emission. These highly fluorescent proteins are unique due to the nature of the covalently attached chromophore, which is composed of modified amino acid residues within the polypeptide.
http://pubs.acs.org/doi/pdf/10.1021/bi00056a003
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