Difference between revisions of "Part:BBa K200013:Design"
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+ | The methionine is shown in RED, the protease recognition site is shown in BLUE and opiorphin is shown in GREEN. The RED & BLUE sections make up the removable linker region cleaved by the serine protease enterokinase. | ||
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Revision as of 15:33, 18 October 2009
Opiorphin + EK cleavage site
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
Since polypeptides can only be biologically synthesised if they start with the amino acid methionine, it has been necessary to design a cleavable peptide sequence starting with methionine. This sequence is found upstream of opiorphin and is enzymatically cleaved following incubation with the enzyme enterokinase. Enterokinase is a highly specific serine protease that cleaves after the recognition sequence Aspartic Acid - Aspartic Acid - Aspartic Acid -Aspartic Acid – Lysine.
The methionine is shown in RED, the protease recognition site is shown in BLUE and opiorphin is shown in GREEN. The RED & BLUE sections make up the removable linker region cleaved by the serine protease enterokinase.
A double stop codon has been incorporated into the sequence to ensure efficient termination.
The sequence has been optimised for expression in E.coli.
Source
Synthetic part.