Difference between revisions of "Part:BBa K5396000"

Revision as of 13:01, 9 September 2024

BaCBM2_RFP_3xMad10

CBM2, or Carbohydrate-Binding Module 2, is a protein sourced from the bacterium Bacillus anthracis. It belongs to a broader family of carbohydrate-binding modules that are crucial for the degradation of polysaccharides. These modules play a vital role in breaking down complex carbohydrates, enabling microorganisms to convert them into usable energy sources. Recent study [ ] has shown that CBM2 has the ability to bind to certain types of plastics, especially those derived from polysaccharides or exhibiting similar structural features. This binding ability is largely due to the protein's carbohydrate-binding properties, which facilitate interactions with specific functional groups found on plastic surfaces.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 597
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K5396000 short</partinfo>
-This is the Carbohydrate Binding Module 2 from Bacillus anthracis fusioned with Red Fluorescent Protein (RFP) and contains a magnetic tag called Mad10.
+CBM2, or Carbohydrate-Binding Module 2, is a protein sourced from the bacterium Bacillus anthracis. It belongs to a broader family of carbohydrate-binding modules that are crucial for the degradation of polysaccharides. These modules play a vital role in breaking down complex carbohydrates, enabling microorganisms to convert them into usable energy sources.
+Recent study [ ] has shown that CBM2 has the ability to bind to certain types of plastics, especially those derived from polysaccharides or exhibiting similar structural features. This binding ability is largely due to the protein's carbohydrate-binding properties, which facilitate interactions with specific functional groups found on plastic surfaces.
 <!-- Add more about the biology of this part here