Difference between revisions of "Part:BBa K3351012"

 
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__NOTOC__
 
__NOTOC__
 
<partinfo>BBa_K3351012 short</partinfo>
 
<partinfo>BBa_K3351012 short</partinfo>
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===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  DCD1L to facilitate attaching of DCD1L on surface and displaying sufficient flexibility of this peptide.
  
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PhaP-linker-DCD1L-HisTag
 
  
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===Reference===
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[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.
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 12:18, 22 October 2020


HisTag-PhaP-linker-DCD1L-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 DCD1L to facilitate attaching of DCD1L on surface and displaying sufficient flexibility of this peptide.


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]