Difference between revisions of "Part:BBa K4438806"

 
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<partinfo>BBa_K4438806 short</partinfo>
  
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MN4_Target_3(BBa_K4438806) is a single-stranded DNA sequence having 82 nucleotides. Figure 1C) shows the secondary structure and minimum free energy. The 5’ end has few bases complementary to MN4_trigger_3_phi29(BBa_K4438805), the middle region has ssDNA sense T7 promoter sequence and the 5’ end has ssDNA sense broccoli sequence.
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===Usage and Biology===
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This part along with MN4_trigger_3_phi29(BBa_K4438805) and Aptamer_MN4(BBa_K4438800) can be used to detect different concentrations of quinine [1].
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K4438806 SequenceAndFeatures</partinfo>
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===Functional Parameters===
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<partinfo>BBa_K4438806 parameters</partinfo>
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===References===
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Reinstein, O., Yoo, M., Han, C., Palmo, T., Beckham, S. A., Wilce, M. C., & Johnson, P. E. (2013). Quinine binding by the cocaine-binding aptamer. Thermodynamic and hydrodynamic analysis of high-affinity binding of an off-target ligand. Biochemistry, 52(48), 8652-8662.

Revision as of 12:35, 12 October 2022

MN4_Target_3

MN4_Target_3(BBa_K4438806) is a single-stranded DNA sequence having 82 nucleotides. Figure 1C) shows the secondary structure and minimum free energy. The 5’ end has few bases complementary to MN4_trigger_3_phi29(BBa_K4438805), the middle region has ssDNA sense T7 promoter sequence and the 5’ end has ssDNA sense broccoli sequence.

Usage and Biology

This part along with MN4_trigger_3_phi29(BBa_K4438805) and Aptamer_MN4(BBa_K4438800) can be used to detect different concentrations of quinine [1].




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]


References

Reinstein, O., Yoo, M., Han, C., Palmo, T., Beckham, S. A., Wilce, M. C., & Johnson, P. E. (2013). Quinine binding by the cocaine-binding aptamer. Thermodynamic and hydrodynamic analysis of high-affinity binding of an off-target ligand. Biochemistry, 52(48), 8652-8662.