Difference between revisions of "Part:BBa K4322000"

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Fibrin is an insoluble protein that is produced in animals in response to bleeding. Fibrin arranges into long fibrous chains that form on the surfaces of activated platelets; together, they produce clots that hinder further blood loss. The polymerization of these long fibrous chains relies on the interaction between N-terminal A- and B-knobs and corresponding a- and b-holes in the γ- and β-modules of fibrin [1].  
 
Fibrin is an insoluble protein that is produced in animals in response to bleeding. Fibrin arranges into long fibrous chains that form on the surfaces of activated platelets; together, they produce clots that hinder further blood loss. The polymerization of these long fibrous chains relies on the interaction between N-terminal A- and B-knobs and corresponding a- and b-holes in the γ- and β-modules of fibrin [1].  
  
This documented part, when fused with protein csgA of the curli operon and chromoproteins, will allow non-covalent crosslinking to occur between chromoprotein csgA fusion nanofibers [2]. The interaction between the knob and hole domain of fibrin-csgA fusion proteins will also allow for increased stability in microbial-ink hydrogel production [2] This part contains the fibrin alpha knob domain.
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This documented part, when fused with protein csgA of the curli operon and chromoproteins, will allow non-covalent crosslinking to occur between chromoprotein csgA fusion nanofibers [2]. The interaction between the knob and hole domain of fibrin-csgA fusion proteins will also allow for increased stability in microbial-ink hydrogel production [2]. This part contains the fibrin gamma hole domain.  
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Revision as of 00:48, 4 October 2022


Fibrin Hole Domain (Gamma)

Fibrin is an insoluble protein that is produced in animals in response to bleeding. Fibrin arranges into long fibrous chains that form on the surfaces of activated platelets; together, they produce clots that hinder further blood loss. The polymerization of these long fibrous chains relies on the interaction between N-terminal A- and B-knobs and corresponding a- and b-holes in the γ- and β-modules of fibrin [1].

This documented part, when fused with protein csgA of the curli operon and chromoproteins, will allow non-covalent crosslinking to occur between chromoprotein csgA fusion nanofibers [2]. The interaction between the knob and hole domain of fibrin-csgA fusion proteins will also allow for increased stability in microbial-ink hydrogel production [2]. This part contains the fibrin gamma hole domain.


References:

[1]R. I. Litvinov et al., “Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions,” Blood, vol. 109, no. 1, pp. 130–138, Jan. 2007, doi: 10.1182/blood-2006-07-033910.

[2]A. M. Duraj-Thatte et al., “Programmable microbial ink for 3D printing of living materials produced from genetically engineered protein nanofibers,” Nat Commun, vol. 12, no. 1, p. 6600, Dec. 2021, doi: 10.1038/s41467-021-26791-x.


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]