Difference between revisions of "Part:BBa K1321152"

 
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Metallothionein fMT (metal-binding peptide) fused N-terminally to CBDcex (a cellulose-binding domain).
 
Metallothionein fMT (metal-binding peptide) fused N-terminally to CBDcex (a cellulose-binding domain).
  
This construct is part of a library of fusions with cellulose binding domains which we designed to bind to cellulose and enable capture of heavy metals ([http://2014.igem.org/Team:Imperial/Functionalisation project page]). Other fusion parts with this metal binding protein can be seen in the table below: [[File:IC14-fMT-part-table.PNG]]
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This construct is part of a library of fusions with cellulose binding domains which we designed to bind to cellulose and enable capture of heavy metals ([http://2014.igem.org/Team:Imperial/Functionalisation project page]). Other fusion parts with this metal binding protein can be seen in the table below: [[File:IC14-fMT-part-table.PNG|center]]
  
 
Note that the start and stop codon, plus 6 bp either side of the sequence, are included the RFC25 prefix and suffix which is not shown.
 
Note that the start and stop codon, plus 6 bp either side of the sequence, are included the RFC25 prefix and suffix which is not shown.
  
 +
For reference, the CBDcex binding affinity to bacterial cellulose has been characterised relative to other sfGFP-CBD fusions, please see [https://parts.igem.org/Part:BBa_K1321342 BBa_K1321342] for details.
  
 
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Latest revision as of 04:52, 2 November 2014

metallothionein Fmt fused to CBDcex

Metallothionein fMT (metal-binding peptide) fused N-terminally to CBDcex (a cellulose-binding domain).

This construct is part of a library of fusions with cellulose binding domains which we designed to bind to cellulose and enable capture of heavy metals ([http://2014.igem.org/Team:Imperial/Functionalisation project page]). Other fusion parts with this metal binding protein can be seen in the table below:
IC14-fMT-part-table.PNG

Note that the start and stop codon, plus 6 bp either side of the sequence, are included the RFC25 prefix and suffix which is not shown.

For reference, the CBDcex binding affinity to bacterial cellulose has been characterised relative to other sfGFP-CBD fusions, please see BBa_K1321342 for details.

Sequence and Features


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]