Difference between revisions of "Part:BBa K5396005"

Latest revision as of 20:33, 1 October 2024

Nt-BaCBM2-Cys

This part is the basic part that composes of N-terminal from Spidroin Nt2RepCt, BBa_K5396002, fused to our BaCBM2-Cys, BBa_K5396003.

Composite part: BBa_K5396010

Usage and Biology

Figure 1. 3D Simulation of Nt-BaCBM2-Cys protein.

Nt2RepCt

Spidroins are the primary proteins that compose spider silk. This part contains the N-terminal domain, which is 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. [1]

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. [2]

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 Biobrick was created through PCR amplification and Gibson Assembly utilizing our composite parts:

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]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K5396005 short</partinfo>
-This part is the N-terminal of Spidroin Nt2RepCt (BBa_K5396002) fused to our BaCBM2-Cys (BBa_K5396003).
+This part is the basic part that composes of N-terminal from Spidroin Nt2RepCt, BBa_K5396002, fused to our BaCBM2-Cys, BBa_K5396003.
+Composite part: <partinfo>BBa_K5396010</partinfo>
 ==Usage and Biology==
+https://static.igem.wiki/teams/5396/registry/imagem-2024-10-01-131943338.png
+'''Figure 1.''' 3D Simulation of Nt-BaCBM2-Cys protein.
 ===Nt2RepCt===
-Spidroins are the primary proteins that compose spider silk. This part contains the N-terminal domain, which is 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 is 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. [https://pubs.acs.org/doi/10.1021/bm401709v]
 ===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.
+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. [https://doi.org/10.1016/j.scitotenv.2023.161948]
 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.