Difference between revisions of "Part:BBa K5396003"
 
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<partinfo>BBa_K5396003 short</partinfo>
 
<partinfo>BBa_K5396003 short</partinfo>
  
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<p>This CBM2 protein is modified with an additional amino acid (cysteine). This enhancement allows it to be effectively utilized in our biosensor technology.</p>
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This CBM2 protein is modified with an additional amino acid (cysteine).
  
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===Usage and Biology===
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=Usage and Biology=
  
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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.
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This CBM2, or Carbohydrate-Binding Module 2, is a protein 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.
  
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Recent study [ ] has shown that CBM2 has the ability to bind to certain types of plastics, especially those derived  exhibiting similar structural features of polysaccharides. This binding ability is largely due to the protein's carbohydrate-binding properties, which facilitate interactions with specific functional groups found on plastic surfaces.
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A recent study has shown that CBM2 has the ability to bind to certain types of plastics, especially those derived  exhibiting similar structural features of polysaccharides. This binding ability is largely due to the protein's carbohydrate-binding properties, which facilitate interactions with specific functional groups found on plastic surfaces. [https://doi.org/10.1016/j.scitotenv.2023.161948]
  
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The cysteine modification allows a strong interaction between the protein and the 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.
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https://static.igem.wiki/teams/5396/registry/bacbm2-3d.png
  
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=== Part Generation ===
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'''Figure 1.''' 3D simulation of the BaCBM2-Cys protein.
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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 our sensor is essential for amplifying the signal of microplastics in electrochemical measurements.
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=Part Generation=
  
 
The BaCBM2-Cys fragment was generated from a PCR reaction using primers that specifically amplify the linker-BaCBM2-linker region of <partinfo>BBa_K5396000</partinfo>
 
The BaCBM2-Cys fragment was generated from a PCR reaction using primers that specifically amplify the linker-BaCBM2-linker region of <partinfo>BBa_K5396000</partinfo>
  
 
The reverse primer used in this reaction adds a codon that encodes the amino acid cysteine at the end of the sequence.
 
The reverse primer used in this reaction adds a codon that encodes the amino acid cysteine at the end of the sequence.
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Latest revision as of 20:30, 1 October 2024


BaCBM2-Cys

This CBM2 protein is modified with an additional amino acid (cysteine).

Usage and Biology

This CBM2, or Carbohydrate-Binding Module 2, is a protein 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.

A recent study has shown that CBM2 has the ability to bind to certain types of plastics, especially those derived exhibiting similar structural features of polysaccharides. This binding ability is largely due to the protein's carbohydrate-binding properties, which facilitate interactions with specific functional groups found on plastic surfaces. [1]

bacbm2-3d.png

Figure 1. 3D simulation of the BaCBM2-Cys protein.

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 our sensor is essential for amplifying the signal of microplastics in electrochemical measurements.

Part Generation

The BaCBM2-Cys fragment was generated from a PCR reaction using primers that specifically amplify the linker-BaCBM2-linker region of BBa_K5396000

The reverse primer used in this reaction adds a codon that encodes the amino acid cysteine at the end of the sequence.

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]