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To subclone and express the nucleocapsid protein in E. coli, the nucleocapsid gene is first amplified by PCR and then inserted into an expression vector, typically one that contains a suitable promoter for expression in E. coli. The recombinant vector is then transformed into E. coli cells, which will produce the nucleocapsid protein when induced by suitable growth conditions. The expressed protein can be purified from the cell lysate using techniques such as affinity chromatography.

Q: Subcloning and expression of nucleocapsid protein in E. coli?
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To subclone and express the nucleocapsid protein in E. coli, the nucleocapsid gene is first amplified by PCR and then inserted into an expression vector, typically one that contains a suitable promoter for expression in E. coli. The recombinant vector is then transformed into E. coli cells, which will produce the nucleocapsid protein when induced by suitable growth conditions. The expressed protein can be purified from the cell lysate using techniques such as affinity chromatography.

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A technique where a long chain of same (homo) nucleotides (polymer) are attached to the 3' OH end. This procedure is very useful for subcloning :

(Suppose the one in bold is the target gene and the other is your vector)

5'------------- AA(An)AA-OH --------------3'

+

3'------------- OH-TT(Tn)TT--------------5'

|

|DNA Ligase permanently joins the fragments together

|

V

5'------------- AA(An)AA------------- 3'

3'--------------TT(Tn)TT--------------5'

The bad part is you can't control the length.

Look up Terminal transferases for more details.

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