Difference between revisions of "Part:BBa K5396003"
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<partinfo>BBa_K5396003 short</partinfo> | <partinfo>BBa_K5396003 short</partinfo> | ||
| − | + | This CBM2 protein is modified with an additional amino acid (cysteine). | |
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| − | + | =Usage and Biology= | |
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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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| + | 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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| + | https://static.igem.wiki/teams/5396/registry/bacbm2-3d.png | ||
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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= | ||
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| + | 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> | ||
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| + | 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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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]
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]