Difference between revisions of "Part:BBa K4989009"

 
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<partinfo>BBa_K4989009 short</partinfo>
 
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==<strong>Application in the field of biology</strong>==
 
==<strong>Application in the field of biology</strong>==
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==<strong>Configuration of the new part</strong>==
 
==<strong>Configuration of the new part</strong>==
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Our new part was created due to the need for a cost-effective and easy way of identifying the colonies that have been transformed with the recombinant plasmid with the correct insert. We thought that it would be an easy way to see if the insert is properly included in the bacterium, although it is not really acurate.
  
  
 
==<strong>The obtainment of the sequence and its difficulties</strong>==
 
==<strong>The obtainment of the sequence and its difficulties</strong>==
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Our sequence came from SnapGene
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https://www.snapgene.com/plasmids/fluorescent_protein_genes_and_plasmids/GFP
  
  

Latest revision as of 15:43, 12 October 2023


GFP

Application in the field of biology

Green Fluorescent Protein (GFP) is a naturally occurring protein that exhibits remarkable fluorescence when exposed to ultraviolet or blue light. The fluorescence of GFP arises from a chemical reaction within the protein. When exposed to UV or blue light, GFP absorbs photons and undergoes a process called fluorescence, where it emits green light. The chromophore, a small molecular group within the protein, is responsible for this fluorescence.GFP revolutionized cell and molecular biology by allowing scientists to visualize and track specific proteins or cells within living organisms.
It has been used to study processes such as gene expression, protein localization, cell migration, and cell division. GFP fusions are created by attaching the GFP gene to the gene of interest, enabling researchers to monitor its expression and localization in real-time. Also, it is commonly used as a reporter gene in molecular biology to assess the activity of promoters or the effectiveness of gene expression. By fusing the GFP gene with a promoter of interest, researchers can easily monitor when and where a gene is active. GFP-tagged proteins have been instrumental in studying protein localization within cells and tracking their movement. This has provided insights into organelle dynamics, vesicle transport, and the functioning of cellular structures.
In genetic studies, GFP has been used to label specific cells or tissues, making it possible to trace the development of embryos, observe the migration of cells, or identify specific cell types. It has played a crucial role in understanding developmental biology and genetics.


Configuration of the new part

Our new part was created due to the need for a cost-effective and easy way of identifying the colonies that have been transformed with the recombinant plasmid with the correct insert. We thought that it would be an easy way to see if the insert is properly included in the bacterium, although it is not really acurate.


The obtainment of the sequence and its difficulties

Our sequence came from SnapGene https://www.snapgene.com/plasmids/fluorescent_protein_genes_and_plasmids/GFP


Biosafety

Our part is safe to be synthesized and utilized on an open bench. Also, the product of the gene does not include any biohazard and does not pose any threat even if by chance there is a leak.



Characterization

Our team, chose for the gold medal to create a new improved part and characterize it as well as possible for the competition standards and the other IGEM teams. So we did not characterize this specific part any further, as something that is crucial to be conducted in the future.


References

[1]Zimmer, Marc. “Green Fluorescent Protein (GFP):  Applications, Structure, and Related Photophysical Behavior.” Chemical Reviews, vol. 102, no. 3, Mar. 2002, pp. 759–82, https://doi.org/10.1021/cr010142r.
[2]Tsien, Roger Y. “THE GREEN FLUORESCENT PROTEIN.” Annual Review of Biochemistry, vol. 67, no. 1, June 1998, pp. 509–44, https://doi.org/10.1146/annurev.biochem.67.1.509.
[3]Chalfie, M. “Green Fluorescent Protein.” Photochemistry and Photobiology, vol. 62, no. 4, 1995, pp. 651–56, https://doi.org/10.1111/j.1751-1097.1995.tb08712.x.