Difference between revisions of "Part:BBa K3582203"

 
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this particular mutant sequence, the amino acid of the Wild type sequence-Glutamic acid is replaced with leucine. As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.
 
this particular mutant sequence, the amino acid of the Wild type sequence-Glutamic acid is replaced with leucine. As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.
  
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[[Image:1 BBa K3582101.png|300px|thumb|center|Figure 1.Structure of the interacting domain of PfEMP1 Protein with inhibitory peptide sequence 1.]]
  
  
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3582203 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3582203 SequenceAndFeatures</partinfo>
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===References===
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1] https://www.rcsb.org/structure/4v3d
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Revision as of 15:09, 22 October 2020


Inhibitory Sequence 1 for EPCR-PfEMP1 Interaction (4V3D)

The following characteristic properties are observed in the inhibitory peptide sequence:

  • 1] Interaction Energy:-5.96088 kcal/mol
  • 2] Stability Value: 7.38979 dG units

This bio brick synthesizes the inhibitory peptide sequence that is believed to bind more efficiently as Compared to the wild type sequence. The peptide sequence is built using saturated mutagenesis. In this particular mutant sequence, the amino acid of the Wild type sequence-Glutamic acid is replaced with leucine. As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.


Figure 1.Structure of the interacting domain of PfEMP1 Protein with inhibitory peptide sequence 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

1] https://www.rcsb.org/structure/4v3d