Difference between revisions of "Part:BBa K3351017"
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<partinfo>BBa_K3351017 short</partinfo>
 
<partinfo>BBa_K3351017 short</partinfo>
 
===Summary===
 
===Summary===
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PhaP contains a hydrophobic granule binding domain and a cytosol-facing hydrophilic domain. PhaP-tagged proteins could interact with various types of hydrophobic surfaces. A (Gly4Ser2)2 flexible linker is inserted between PhaP and  P6.2 to facilitate attaching of P6.2 on surface and displaying sufficient flexibility of this peptide.  
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PhaP contains a hydrophobic granule binding domain and a cytosol-facing hydrophilic domain. PhaP-tagged proteins could interact with various types of hydrophobic surfaces. A (Gly4Ser2)2 flexible linker is inserted between PhaP and  P6.2 to facilitate attaching of P6.2 on surface and displaying sufficient flexibility of this peptide. TESTING
  
  

Revision as of 06:57, 23 October 2020


HisTag-PhaP-linker-P6.2-HisTag

Summary

PhaP contains a hydrophobic granule binding domain and a cytosol-facing hydrophilic domain. PhaP-tagged proteins could interact with various types of hydrophobic surfaces. A (Gly4Ser2)2 flexible linker is inserted between PhaP and P6.2 to facilitate attaching of P6.2 on surface and displaying sufficient flexibility of this peptide. TESTING


Reference

[1] Xue Q, Liu XB, Lao YH, Wu LP, Wang D, Zuo ZQ, Chen JY, Hou J, Bei YY, Wu XF, Leong KW, Xiang H, Han J. Anti-infective biomaterials with surface-decorated tachyplesin I. Biomaterials. 2018 Sep;178:351-362. doi: 10.1016/j.biomaterials.2018.05.008. Epub 2018 May 9. PMID: 29778319. 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]