Difference between revisions of "Part:BBa K5023001"

 
 
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<partinfo>BBa_K5023001 short</partinfo>
 
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Linker, the most basic function of linkers in recombinant proteins is to covalently join functional domains (e.g., flexible linkers or rigid linkers) or release them under desired conditions (clickable linkers). Linkers can also provide many derived functions, such as improving the folding and stability of recombinant proteins, enhancing the expression of fusion proteins, and they can enhance the bioactivity of fusion proteins.  
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Linker, the most basic function of linkers in recombinant proteins is to covalently join functional domains (e.g., flexible linkers or rigid linkers) or release them under desired conditions (clickable linkers). Linkers can also provide many derived functions, such as improving the folding and stability of recombinant proteins, enhancing the expression of fusion proteins, and they can enhance the bioactivity of fusion proteins. The linker we chose binds to the C-terminal region of MHETase to the N-terminal of PETase, with flexible glycine-serine linkers of 12 total residues (Gly-Gly-Gly-Ser-Gly-Gly-Ser-Gly-Gly-Gly-Ser-Gly). 
  
 
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<partinfo>BBa_K5023001 parameters</partinfo>
 
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===References===
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KNOTT, B. C. et al. Characterization and engineering of a two-enzyme system for plastics depolymerization. Proceedings of the National Academy of Sciences of the United States of America, v. 117, n. 41, p. 25476–25485, 13 out. 2020. https://doi.org/10.1073/pnas.2006753117
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CHEN, X.; ZARO, J. L.; SHEN, W.-C. Fusion protein linkers: Property, design and functionality. Advanced Drug Delivery Reviews, v. 65, n. 10, p. 1357–1369, out. 2013. http://dx.doi.org/10.1016/j.addr.2012.09.039

Latest revision as of 19:21, 8 October 2023


Linker (12aa)

Linker, the most basic function of linkers in recombinant proteins is to covalently join functional domains (e.g., flexible linkers or rigid linkers) or release them under desired conditions (clickable linkers). Linkers can also provide many derived functions, such as improving the folding and stability of recombinant proteins, enhancing the expression of fusion proteins, and they can enhance the bioactivity of fusion proteins. The linker we chose binds to the C-terminal region of MHETase to the N-terminal of PETase, with flexible glycine-serine linkers of 12 total residues (Gly-Gly-Gly-Ser-Gly-Gly-Ser-Gly-Gly-Gly-Ser-Gly).

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

KNOTT, B. C. et al. Characterization and engineering of a two-enzyme system for plastics depolymerization. Proceedings of the National Academy of Sciences of the United States of America, v. 117, n. 41, p. 25476–25485, 13 out. 2020. https://doi.org/10.1073/pnas.2006753117

CHEN, X.; ZARO, J. L.; SHEN, W.-C. Fusion protein linkers: Property, design and functionality. Advanced Drug Delivery Reviews, v. 65, n. 10, p. 1357–1369, out. 2013. http://dx.doi.org/10.1016/j.addr.2012.09.039