Difference between revisions of "Part:BBa K1995002"
 
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<partinfo>BBa_K1995002 short</partinfo>
 
<partinfo>BBa_K1995002 short</partinfo>
  
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PHG (INP-N-HG)
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Based on BBa_K1995000 (BHG), we added INP-N to the upstream of BHG. Using INP-N, we anchored BHG out of the outer membrane of E.coli in
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  Based on BBa_K1995000 (BHG), we added INP-N to the upstream of BHG. Using INP-N, we anchored BHG out of the outer membrane of E.coli in order to increase the binding efficiency of cupric and mercuric ions.
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order to increase the binding efficiency of cupric and mercuric ions.
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==Ice nucleation protein (INP)==
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To increase the binding efficiency and detect the concentration of heavy metals, we used INP to anchor BHG out of the outer membrane of E. coli. 
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Ice nucleation protein (INP) is an excretion surface protein. It is widely used for establishing germ surface display system. It contains an internal repeated domain (IRD) and an N-terminal anchoring domain (fig.1). Studies have shown that decrease the time of repetition of IRD can also get a better-off rate of displaying. So we decreased the time of repetition of IRD to reduce pressure of synthesis of E. coli.
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[[File:INP.png]]
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==Binding heavy metals==
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We detect the binding efficiency of PHG and other parts and get the following chart. (Fig. 2)
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[[File:0022.png]]
  
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'''Ice nucleation protein (INP)'''
 
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  To increase the binding efficiency and detect the concentration of heavy metals, we used INP to anchor BHG out of the outer membrane of E. coli.
 
−
  Ice nucleation protein (INP) is an excretion surface protein. It is widely used for establishing germ surface display system. It contains an internal repeated domain (IRD) and an N-terminal anchoring domain (fig.1). Studies have shown that decrease the time of repetition of IRD can also get a better-off rate of displaying. So we decreased the time of repetition of IRD to reduce pressure of synthesis of E. coli.
 
  
  
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<span class='h3bb'>Sequence and Features</span>
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<span class='h3bb'>'''Sequence and Features'''</span>
 
<partinfo>BBa_K1995002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1995002 SequenceAndFeatures</partinfo>
  

Latest revision as of 18:30, 15 October 2016


PHG (INP-N-HG)

Based on BBa_K1995000 (BHG), we added INP-N to the upstream of BHG. Using INP-N, we anchored BHG out of the outer membrane of E.coli in order to increase the binding efficiency of cupric and mercuric ions.

Ice nucleation protein (INP)

To increase the binding efficiency and detect the concentration of heavy metals, we used INP to anchor BHG out of the outer membrane of E. coli.

Ice nucleation protein (INP) is an excretion surface protein. It is widely used for establishing germ surface display system. It contains an internal repeated domain (IRD) and an N-terminal anchoring domain (fig.1). Studies have shown that decrease the time of repetition of IRD can also get a better-off rate of displaying. So we decreased the time of repetition of IRD to reduce pressure of synthesis of E. coli.

INP.png

Binding heavy metals

We detect the binding efficiency of PHG and other parts and get the following chart. (Fig. 2)

0022.png


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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 429
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI.rc site found at 238