Difference between revisions of "Part:BBa K3582013"
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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 phenylalanine(F). 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 phenylalanine(F). As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength. | ||
− | [[Image:Inhibitory sequence 2.png|900px|thumb|center|Figure 1. DNA sequence of the inhibitory peptide sequence with its translation output.]] | + | [[Image:Inhibitory sequence 2.png|900px|thumb|center|Figure 1. DNA sequence of the inhibitory peptide sequence 2 with its translation output.]] |
− | [[Image:Is22 BBa K3582013.png|400px|thumb|center|Figure 1.Interacting regions of the PfEMP1 CIDRa domain and the inhibitory peptide sequence | + | [[Image:Is22 BBa K3582013.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.]] |
Latest revision as of 08:11, 18 October 2020
Inhibitory Peptide sequence 2 for CD36-PfEMP CIDRa Domain
The following characteristic properties are observed in the inhibitory peptide sequence:
- 1]Interaction Energy: - 18.7332 kcal/mol
- 2]Stability Value:4.623 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 phenylalanine(F). As a result, an upgradation in its interactive properties is observed that is thought to improve its binding strength.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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