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Bacteria Transformation and Protein Electrophoresis Paragraphs<br />In the first part of the workshop we genetically transformed the bacteria E. Coli. Bacteria are unicellular organism with their genetic material at the center of it. They contain other circular DNA strands called plasmids. With the insertion of a plasmid with a desired gene (pGLO), the bacteria are transformed. We inserted a plasmid encoding for green fluorescent protein (GFP) in the E. Coli and with the use of a sugar, arabinose, the gene is activated and the protein is produced. The bacteria with the pGLO and arabinose solution produced the fluorescent protein and the bacteria without arabinose did not.<br />The next part of the workshop we worked with a technique called electrophoresis. We used the bacteria that produced GFP and the ones that did not. Using a Laemmli buffer, the bacteria was open and the proteins were denaturalized and coated with a negative charge. This was done by the SDS compound in the buffer. With the electrophoresis the proteins run downward to the positive charged probe and get separated by their sizes in the process. The GFP protein size is 37kd and with the use of a ladder, a reference with known sizes, we identified the protein. <br />

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Bacteria transformation and protein electrophoresis paragraphs

  • 1. Bacteria Transformation and Protein Electrophoresis Paragraphs<br />In the first part of the workshop we genetically transformed the bacteria E. Coli. Bacteria are unicellular organism with their genetic material at the center of it. They contain other circular DNA strands called plasmids. With the insertion of a plasmid with a desired gene (pGLO), the bacteria are transformed. We inserted a plasmid encoding for green fluorescent protein (GFP) in the E. Coli and with the use of a sugar, arabinose, the gene is activated and the protein is produced. The bacteria with the pGLO and arabinose solution produced the fluorescent protein and the bacteria without arabinose did not.<br />The next part of the workshop we worked with a technique called electrophoresis. We used the bacteria that produced GFP and the ones that did not. Using a Laemmli buffer, the bacteria was open and the proteins were denaturalized and coated with a negative charge. This was done by the SDS compound in the buffer. With the electrophoresis the proteins run downward to the positive charged probe and get separated by their sizes in the process. The GFP protein size is 37kd and with the use of a ladder, a reference with known sizes, we identified the protein. <br />