Difference between revisions of "Part:BBa K3582014"

 
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This biobrick 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 last amino acid of the Wild type sequence-Serine(S) is replaced with tryptophan(W). As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.
 
This biobrick 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 last amino acid of the Wild type sequence-Serine(S) is replaced with tryptophan(W). As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.
  
[[Image:Is3 BBa K3582014.png|900px|thumb|center|Figure 1. DNA sequence of the inhibitory peptide sequence 2 with its translation output.]]
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[[Image:Is3 BBa K3582014.png|900px|thumb|center|Figure 1. DNA sequence of the inhibitory peptide sequence 3 with its translation output.]]
  
  
  
[[Image:Is33 BBa K3582014.png|400px|thumb|center|Figure 1.Interacting regions of the PfEMP1 CIDRa domain and the inhibitory peptide sequence 2 shown here in protein ribbon model.]]
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[[Image:Is33 BBa K3582014.png|400px|thumb|center|Figure 1.Interacting regions of the PfEMP1 CIDRa domain and the inhibitory peptide sequence 3 shown here in protein ribbon model.]]
  
  

Latest revision as of 08:31, 18 October 2020


Inhibitory Peptide sequence 3 for CD36-PfEMP CIDRa Domain

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

  • 1]Interaction Energy: - 18.466 kcal/mol
  • 2]Stability Value:4.819 dG units

This biobrick 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 last amino acid of the Wild type sequence-Serine(S) is replaced with tryptophan(W). As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.

Figure 1. DNA sequence of the inhibitory peptide sequence 3 with its translation output.


Figure 1.Interacting regions of the PfEMP1 CIDRa domain and the inhibitory peptide sequence 3 shown here in protein ribbon model.



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] The structural basis for CD36 binding by the malaria parasite.

Fu-Lien Hsieh1, Louise Turner2, Jani Reddy Bolla3, Carol V. Robinson3, Thomas Lavstsen2 & Matthew K. Higgins1