Difference between revisions of "Part:BBa K5396005"
Jocomodaro (Talk | contribs) (→Usage and Biology) |
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<partinfo>BBa_K5396005 short</partinfo> | <partinfo>BBa_K5396005 short</partinfo> | ||
| − | This part is the N-terminal of Spidroin fused to our BaCBM2 | + | This part is the N-terminal of Spidroin Nt2RepCt (BBa_K5396002) fused to our BaCBM2-Cys (BBa_K5396003). |
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| + | ==Usage and Biology== | ||
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| + | ===Nt2RepCt== | ||
| − | |||
Spidroins are the primary proteins that compose spider silk. This part contains the N-terminal domain, which s involved in the initial formation of silk fibers and is crucial for the protein's solubility and stability, and is fused to the BaCBM2 protein, that has the ability to bind to plastics. | Spidroins are the primary proteins that compose spider silk. This part contains the N-terminal domain, which s involved in the initial formation of silk fibers and is crucial for the protein's solubility and stability, and is fused to the BaCBM2 protein, that has the ability to bind to plastics. | ||
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| + | ===BaCBM2-Cys=== | ||
| + | |||
| + | This CBM2, or Carbohydrate-Binding Module 2, is a protein sourced from Bacillus anthracis. It belongs to a broader family of carbohydrate-binding modules that are crucial for the degradation of polysaccharides. These modules are important to break down complex carbohydrates, enabling microorganisms to convert them into usable energy sources. | ||
| + | |||
| + | The cysteine modification allows a strong interaction between the protein and our sensor surface, due to the affinity between the SH group and the Au(111) surface. This increase in interaction with the sensor is essential for amplifying the signal of microplastics in electrochemical measurements. | ||
===Part Generation=== | ===Part Generation=== | ||
| − | Gibson | + | |
| + | This part was generated by amplifying by PCR and Gibson Assembly using our composite parts: | ||
| + | *<partinfo>BBa K5396007</partinfo> | ||
| + | *<partinfo>BBa K5396009</partinfo> | ||
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Revision as of 18:59, 25 September 2024
Nt-BaCBM2-Cys
This part is the N-terminal of Spidroin Nt2RepCt (BBa_K5396002) fused to our BaCBM2-Cys (BBa_K5396003).
Usage and Biology
=Nt2RepCt
Spidroins are the primary proteins that compose spider silk. This part contains the N-terminal domain, which s involved in the initial formation of silk fibers and is crucial for the protein's solubility and stability, and is fused to the BaCBM2 protein, that has the ability to bind to plastics.
BaCBM2-Cys
This CBM2, or Carbohydrate-Binding Module 2, is a protein sourced from Bacillus anthracis. It belongs to a broader family of carbohydrate-binding modules that are crucial for the degradation of polysaccharides. These modules are important to break down complex carbohydrates, enabling microorganisms to convert them into usable energy sources.
The cysteine modification allows a strong interaction between the protein and our sensor surface, due to the affinity between the SH group and the Au(111) surface. This increase in interaction with the sensor is essential for amplifying the signal of microplastics in electrochemical measurements.
Part Generation
This part was generated by amplifying by PCR and Gibson Assembly using our composite parts:
- No part name specified with partinfo tag.
- No part name specified with partinfo tag.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]