This lab report went much more smoothly than the previous one. I feel as though my report had a much better flow, and I hope that shows when you are reading it. I believe I was able to properly format my report this time around, which should contribute to the flow of the report and make it easier to follow. My introduction contains more background information and better prepares the reader for what follows. I also believe that more discussion is much more thoughtful and properly sums up the report.
Aequorea victoria is a species of jellyfish often found off the coast of North America in the Pacific Ocean1. Like many Cnidarians, A. victoria is capable of producing bioluminescence. This is accomplished through the action of two proteins, aeqourin and green fluorescent protein (GFP). In A. victoria, aeqourin binds with calcium and gives off a blue light. The blue light is absorbed by GFP causing the protein to fluoresce green. The action of these proteins allow A. Victoria to produce light1. The fluorescent properties of GFP have become enormously useful in a research setting. The GFP gene is very versatile and can be inserted and expressed in almost any organism. Since the protein is fluorescent in UV light, it is often used as a biomarker in order to tag and study different genes and cell processes1,2.
GFP is a 27Kda protein consisting of 11 beta strands that form a beta-barrel. The structure that is responsible for the green fluorescence emitted by the protein, called the chromophore, is located in the middle of the beta-barrel3. The chromohpore is analogous to the active site of an enzyme, in that the protein folds in a specific fashion that allows for the chromophore residues to come together. Since GFP actually forms its own chromophore, there are no cofactors required for fluorescence. This also mean that if the protein is denatured fluorescence will be lost. GFP remains stable in a number of harsh conditions...