BerkiGEM2007Present1
From 2007.igem.org
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Over the summer I investigated and created two alternatives to the hemoglobin part in our device. I worked with two genes we believed might allow our blood to carry more oxygen than hemoglobin. | Over the summer I investigated and created two alternatives to the hemoglobin part in our device. I worked with two genes we believed might allow our blood to carry more oxygen than hemoglobin. | ||
| - | The first gene I will | + | The first gene I will discuss is H-NOX (Heme-Nitric oxide and Oxygen bonding). H-NOX is a heme-based sensor that is found in bacteria. H-NOX is able to bond to Oxygen using a distal pocket tyrosine. For this gene I added the T7 promoter we created for this project, an RBS site, and lastly a Bca1092 terminator. As I said previously this part would replace the hemoglobin part in our final device. When I assayed this part the results were inconclusive. The part was assembled correctly but the assay didn't show strong signs of expression. |
The second gene I explored was Sperm Whale Myoglobin. Myoglobin is a monomeric protein that behaves as an intracellular oxygen storage site. Sperm whale myoglobin in particular is easily found in large amounts in the whale's muscle tissue. The construction of this part was very similar to that of the H-NOX composite part. Used the same promoter, terminator, and RBS. The assay for Myoglobin showed a bit more promise but couldn't conclusively show that Myoglobin was binding to oxygen. | The second gene I explored was Sperm Whale Myoglobin. Myoglobin is a monomeric protein that behaves as an intracellular oxygen storage site. Sperm whale myoglobin in particular is easily found in large amounts in the whale's muscle tissue. The construction of this part was very similar to that of the H-NOX composite part. Used the same promoter, terminator, and RBS. The assay for Myoglobin showed a bit more promise but couldn't conclusively show that Myoglobin was binding to oxygen. | ||
Revision as of 02:15, 22 September 2007
Hannah Cole- Alternatives To Hemoglobin:
Over the summer I investigated and created two alternatives to the hemoglobin part in our device. I worked with two genes we believed might allow our blood to carry more oxygen than hemoglobin.
The first gene I will discuss is H-NOX (Heme-Nitric oxide and Oxygen bonding). H-NOX is a heme-based sensor that is found in bacteria. H-NOX is able to bond to Oxygen using a distal pocket tyrosine. For this gene I added the T7 promoter we created for this project, an RBS site, and lastly a Bca1092 terminator. As I said previously this part would replace the hemoglobin part in our final device. When I assayed this part the results were inconclusive. The part was assembled correctly but the assay didn't show strong signs of expression.
The second gene I explored was Sperm Whale Myoglobin. Myoglobin is a monomeric protein that behaves as an intracellular oxygen storage site. Sperm whale myoglobin in particular is easily found in large amounts in the whale's muscle tissue. The construction of this part was very similar to that of the H-NOX composite part. Used the same promoter, terminator, and RBS. The assay for Myoglobin showed a bit more promise but couldn't conclusively show that Myoglobin was binding to oxygen.
