Difference between revisions of "Part:BBa K2309025:Design"

 
(Design Notes)
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===Design Notes===
 
===Design Notes===
blackbass genomic DNA
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Grammistins are a group of peptides secreted by soapfishes and characterized by its amphiphilic -helical structure. There are four types of Grammistins: Pp1,Pp3, Gs1, and Gs2. Gs 1 and Gs 2 are from Grammistes sexlineatus and Pp 1 and Pp 3 from Pogonoperca punctata (Yokota, Nagashima, and Shiom, 2001). Grammistin-Pp1 is made up of thirteen amino acid residues. Studies showed that Grammistin-Pp1 could interact with phospholipids and influence the permeability of membrane. Sugiyama et al. (2006) reported that the peptide Grammistin-Pp1 is effective on both Gram negative bacteria and Gram positive bacteria, which includes Staphylococcus aureus.
 
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===Source===
 
===Source===

Revision as of 08:29, 1 November 2017


Grammistin-Pp1 for Lactococcus lactis NZ9000 (codon optimized)


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

Grammistins are a group of peptides secreted by soapfishes and characterized by its amphiphilic -helical structure. There are four types of Grammistins: Pp1,Pp3, Gs1, and Gs2. Gs 1 and Gs 2 are from Grammistes sexlineatus and Pp 1 and Pp 3 from Pogonoperca punctata (Yokota, Nagashima, and Shiom, 2001). Grammistin-Pp1 is made up of thirteen amino acid residues. Studies showed that Grammistin-Pp1 could interact with phospholipids and influence the permeability of membrane. Sugiyama et al. (2006) reported that the peptide Grammistin-Pp1 is effective on both Gram negative bacteria and Gram positive bacteria, which includes Staphylococcus aureus.

Source

This part is optimized from part BBa_K1162003. The original part BBa_K1162003, actually, is suitable for Escherichia coli. This part has optimized codon usage which applicable to Lactococcus lactis NZ9000 strain

References