Green Fluorescent Protein - Essay Example

This generates a plethora of chemical transformations where glycine forms a chemical bond with serine, as a result a new closed ring is formed, and the process is followed by dehydration. In the next hour, environmental oxygen reacts with the bond in tyrosine resulting in the formation of double bond to form a new fluorescent chromophore. GFP is ideal for genetic engineering as it has its own chromophore. Genetic instructions are provided to the cell under investigation, which eventually builds the GFP protein, GFP folds up in a specific manner and glows.

Various research studies involve GFP as a reporter molecule to understand the functioning of genes or molecules in an explicit manner. Green Fluorescent Protein (GFP) is a protein molecule generated by a jellyfish Aequorea victoria. The organism displays its fluorescent protein along the margin of its umbrella as the glowing points of light. The light is generated from the yellow tissue masses encompassing approximately 6000-7000 photogenic cells. These photogenic cells produce light by means of bioluminescence, encompassing a calcium-activated photoprotein, popularly known as “aequorin” that produces green fluorescent protein (GFP) and blue-green light.

GFP accepts energy from the protein molecule aequorin and gives out as green light (Green Fluorescent Protein, n.d.). GFP comprises of 238 amino acids in its protein. The protein remains highly stable in neutral buffers even at the temperature of 65ºC. GFP is also stable at wider pH range from 5.5 to 12. The protein molecule of GFP is strongly fluorescent, with a quantum effectiveness of about 80 percent as well as displays molar extinction coefficient of 2.2 x 104 cm-1 M-1. Maximum fluorescence displayed by GFP is at 400 nm while lesser peak is displayed at 475nm, whereas the fluorescence emission peak is displayed at 509nm.

The intrinsic fluorescence of the GFP is attributed to its exclusive covalently bound chromophore, which is